Characterization of Neurospora crassa Tom40-deficient Mutants and Effect of Specific Mutations on Tom40 Assembly

The TOM complex (Translocase of the Outer mitochondrialMembrane) is responsible for the recognition of mitochondrial preproteins synthesized in the cytosol and for their translocation across or into the outer mitochondrial membrane. Tom40 is the major component of the TOM complex and forms the translocation pore. We have created a tom40 mutant of Neurospora crassa and have demonstrated that the gene is essential for the viability of the organism. Mitochondria with reduced levels of Tom40 were deficient for import of mitochondrial preproteins and contained reduced levels of the TOM complex components Tom22 and Tom6, suggesting that the import and/or stability of these proteins is dependent on the presence of Tom40. Mutant Tom40 preproteins were analyzed for their ability to be assembled into the TOM complex. In vitroimport assays revealed that conserved regions near the N terminus (residues 51–60) and the C terminus (residues 321–323) of the 349-amino acid protein were required for assembly beyond a 250-kDa intermediate form. Mutant strains expressing Tom40 with residues 51–60 deleted were viable but exhibited growth defects. Slow growing mutants expressing Tom40, where residues 321–323 were changed to Ala residues, were isolated but showed TOM complex defects, whereas strains in which residues 321–323 were deleted could not be isolated. Analysis of the assembly of mutant Tom40 precursors in vitro supported a previous model in which Tom40 precursors progress from the 250-kDa intermediate to a 100-kDa form and then assemble into the 400-kDa TOM complex. Surprisingly, when wild type mitochondria containing Tom40 precursors arrested at the 250-kDa intermediate were treated with sodium carbonate, further assembly of intermediates into the TOM complex occurred, suggesting that disruption of protein-protein interactions may facilitate assembly. Import of wild type Tom40 precursor into mitochondria containing a mutant Tom40 lacking residues 40–48 revealed an alternate assembly pathway and demonstrated that the N-terminal region of pre-existing Tom40 molecules in the TOM complex plays a role in the assembly of incoming Tom40 molecules. The TOM complex (Translocase of the Outer mitochondrialMembrane) is responsible for the recognition of mitochondrial preproteins synthesized in the cytosol and for their translocation across or into the outer mitochondrial membrane. Tom40 is the major component of the TOM complex and forms the translocation pore. We have created a tom40 mutant of Neurospora crassa and have demonstrated that the gene is essential for the viability of the organism. Mitochondria with reduced levels of Tom40 were deficient for import of mitochondrial preproteins and contained reduced levels of the TOM complex components Tom22 and Tom6, suggesting that the import and/or stability of these proteins is dependent on the presence of Tom40. Mutant Tom40 preproteins were analyzed for their ability to be assembled into the TOM complex. In vitroimport assays revealed that conserved regions near the N terminus (residues 51–60) and the C terminus (residues 321–323) of the 349-amino acid protein were required for assembly beyond a 250-kDa intermediate form. Mutant strains expressing Tom40 with residues 51–60 deleted were viable but exhibited growth defects. Slow growing mutants expressing Tom40, where residues 321–323 were changed to Ala residues, were isolated but showed TOM complex defects, whereas strains in which residues 321–323 were deleted could not be isolated. Analysis of the assembly of mutant Tom40 precursors in vitro supported a previous model in which Tom40 precursors progress from the 250-kDa intermediate to a 100-kDa form and then assemble into the 400-kDa TOM complex. Surprisingly, when wild type mitochondria containing Tom40 precursors arrested at the 250-kDa intermediate were treated with sodium carbonate, further assembly of intermediates into the TOM complex occurred, suggesting that disruption of protein-protein interactions may facilitate assembly. Import of wild type Tom40 precursor into mitochondria containing a mutant Tom40 lacking residues 40–48 revealed an alternate assembly pathway and demonstrated that the N-terminal region of pre-existing Tom40 molecules in the TOM complex plays a role in the assembly of incoming Tom40 molecules. translocase of the outer mitochondrial membrane translocases of the inner mitochondrial membrane repeat induced point mutation inactivated by repeat induced point mutation blue native gel electrophoresis polyvinylidene difluoride Most mitochondrial proteins are nuclear gene products that must be synthesized on cytosolic ribosomes, imported into mitochondria, and sorted to the correct mitochondrial subcompartment. These processes require the concerted action of complex protein translocases located in the outer and inner mitochondrial membranes (1Pfanner N. Geissler A. Nat. Rev. Mol. Cell. Biol. 2001; 2: 339-349Crossref PubMed Scopus (421) Google Scholar, 2Paschen S. Neupert 2001; Google Scholar, N. N. Rev. Mol. Biol. 2001; PubMed Scopus Google The of mitochondrial preproteins into the is by the TOM complex (Translocase of the Outer which mitochondrial preproteins in the The TOM complex the of preproteins to the outer membrane the of preproteins for the inner mitochondrial across the outer membrane. import and of these preproteins the action of the of the mitochondrial The Neurospora crassa TOM complex Tom40, S. S. Neupert Cell. PubMed Scopus Google Scholar, Neupert S. Biol. PubMed Scopus Google and and proteins are in the TOM which and Rev. PubMed Scopus Google Scholar, N. A. Rev. Biol. PubMed Scopus Google The cytosolic of and for mitochondrial precursor The of the complex Tom6, and form the TOM which is to the Neupert S. Biol. PubMed Scopus Google Scholar, A. N. Mol. Cell. Biol. PubMed Scopus Google Scholar, A. N. Mol. Cell. Biol. 2001; PubMed Scopus Google The the major point for precursors mitochondria N. Neupert Cell. PubMed Scopus Google Scholar, A. N. Mol. Cell. Biol. PubMed Scopus Google Scholar, A. Neupert PubMed Scopus Google Scholar, S. Biol. PubMed Scopus Google Scholar, S. PubMed Scopus Google Scholar, N. Mol. Biol. Cell. PubMed Scopus Google Tom40 to be an essential protein in S. A. PubMed Scopus Google The protein be to precursor proteins the translocation A. PubMed Scopus Google Scholar, N. Neupert PubMed Scopus Google and is the major component of the TOM complex in S. and N. crassa S. S. Neupert Cell. PubMed Scopus Google Scholar, N. PubMed Scopus Google Scholar, Neupert Biol. PubMed Scopus Google on to Tom40 may form the major of the precursor on the of the outer membrane and to on the cytosolic of the membrane Neupert Biol. PubMed Scopus Google TOM complex and containing Tom40 have and N. PubMed Scopus Google Scholar, Neupert S. Biol. 2001; PubMed Scopus Google The TOM complex to be in by and S. S. Neupert Cell. PubMed Scopus Google Scholar, Neupert S. Biol. PubMed Scopus Google Scholar, N. PubMed Scopus Google Scholar, Neupert S. Biol. 2001; PubMed Scopus Google A. S. A. PubMed Scopus Google In the TOM Tom40 an with the Neupert S. Biol. PubMed Scopus Google Scholar, A. N. Mol. Cell. Biol. PubMed Scopus Google Scholar, Neupert Mol. Cell. Biol. Scopus Google Scholar, N. Mol. Biol. PubMed Scopus Google have precursors the and the that the interactions Tom40 molecules and Tom40 and TOM complex components Neupert Mol. Cell. Biol. Scopus Google of Tom40 have that the N and C into the is with that be by but when the mitochondrial membrane is to the to the Neupert Biol. PubMed Scopus Google The of the to a to Neupert Google Scholar, PubMed Google with the mitochondrial outer membrane. of in Tom40 in and from N. PubMed Scopus Google but of Tom40 from mitochondria revealed and Neupert S. Biol. 2001; PubMed Scopus Google The and assembly of Tom40 into the mitochondrial outer membrane the TOM complex and is the protein in a Neupert Biol. PubMed Scopus Google of Tom40 into the TOM complex is to translocation intermediates Neupert Biol. PubMed Scopus Google Scholar, N. N. Nat. Biol. 2001; PubMed Scopus Google Scholar, Scopus Google In the of the Tom40 precursor at the outer of the TOM complex a is imported the outer membrane and assembled on the of the membrane into an intermediate of that pre-existing molecules of Tom40 and are for the by which Tom40 into the outer membrane. In when the precursor that is with components in the 250-kDa intermediate to a 100-kDa intermediate that Tom40 a of the imported and a pre-existing intermediate further assembly and with proteins to the assembled TOM complex N. N. Nat. Biol. 2001; PubMed Scopus Google In a Tom40 to into the membrane from the 250-kDa form into the 400-kDa assembled complex Neupert Biol. PubMed Scopus Google conserved of acid residues near the N terminus of Tom40 is required for assembly and stability of Tom40 the TOM but is not in of synthesized Tom40 to mitochondria Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google of lacking of the protein were to mitochondrial precursors in the cytosol and lacking a of the gene were A. PubMed Scopus Google and the of Tom40 in have a of the gene in N. crassa that is in a We have further the assembly pathway of Tom40 into the TOM complex. and crassa strains Scopus Google in are in were in or but an of of with containing tom40 type an of of tom40 tom40 an with a of of with tom40 tom40 an of tom40 with a of of with tom40 tom40 an with a of 51–60 and a in from to of with tom40 tom40 an with residues at 321–323 changed to of with in a induced point mutation in N. crassa when of the in a a in the of to in of the Rev. PubMed Scopus Google Tom40 to be an essential protein in N. the of to the tom40 that containing are in a that with a wild type of the The and strains for are in Scholar, Neupert PubMed Google Neurospora Scholar, S. A. PubMed Scopus Google a revealed that gene located on of N. a of of the for were with a and of tom40 were on and strains containing were by to the from that were of growth on were to be of the wild type with to Tom40 whereas the could or wild type tom40 The is in from the were for the with the in were in containing and from to the to the to to the a the growth Tom40 could not be by the which these analyzed in to the gene at the tom40 the in the of the gene were by The gene at the and of a at were of the were from and were that created a at the to the Neupert Google Scholar, PubMed Google of the and these to be We have the of for mutants expressing of Tom40 in a previous Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google crassa S. A. PubMed Scopus Google Mol. Cell. Biol. PubMed Scopus Google or by of of a Scholar, were with and in at a of to in a of with of in a and for on with of the of and the were to for at of the were to containing for of and the containing the The for of strains expressing mutant of Tom40 Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google mutant were by of from a containing a of N. crassa tom40 and a gene PubMed Scopus Google to the were into to strains expressing in contained in the region residues and of crassa Tom40 and the residues, or of residues a Tom40 where residues at 321–323 were changed to were on containing and for of the and to the action of of on the and for to and mutant of Tom40 to a for The presence of mutant in the by products from into Mutant were created by and for in vitro and to mutant Tom40 precursor proteins for import into isolated in vitro import the of mitochondria A. Neupert Biol. PubMed Scopus Google import of Tom40 precursors Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google and import of mitochondrial precursor proteins Neupert Biol. PubMed Scopus Google were Import analyzed by or blue native gel electrophoresis and were by to imported precursor proteins were into Mitochondria were in sodium for at The at in a for at and the were for Mitochondria were in of containing or in at for and a of in and the analyzed on a blue native gel PubMed Scopus Google Scholar, PubMed Scopus Google of from in for at by with The then in sodium containing and The were by at in a and were in the a on were in and for on were then in at The of and were by the of of were in a The of gel and of of of of and the a of and to were in and The were the or of with the of mitochondrial proteins by gel electrophoresis PubMed Scopus Google PubMed Google and protein with the and a with a and the precursor proteins for import were by in vitro and with the in the presence of Tom40 is the major component of the mitochondrial outer membrane translocation Neupert S. Biol. 2001; PubMed Scopus Google and is an essential gene in A. PubMed Scopus Google the of to N. crassa The of the a in which the tom40 gene in is inactivated by whereas the a wild type of the gene revealed that the tom40 of the gene and tom40 is an essential gene by were containing the of in the and crassa are and the of of into for the tom40 for the and containing tom40 is be of of isolated from these revealed that were were and were the tom40 that the of were to the tom40 the with a containing a wild type of on containing and viable strains were these that tom40 is an essential gene in N. The in with to and which to to the by growth in containing and these the growth of reduced the tom40 to levels of Tom40 when in the Analysis of mitochondrial proteins in these showed the in Tom40 of the TOM complex from mitochondria revealed in or stability that the complex forms in the mutant but is reduced in Mitochondria deficient in Tom40 were with to the levels of mitochondrial of the TOM complex. The of the TOM proteins and the mitochondrial proteins and were by the in Tom40 the of the TOM complex Tom22 and Tom6, were reduced the that the Tom40 a of of and analyzed for the presence of The of tom40 is reduced in where the that have or PubMed Scopus Google Scholar, A. Neupert PubMed Scopus Google We were to a for in or mutant suggesting that are and/or that are were in in that the levels of and by Tom6, were not to levels of the that the import and/or stability of Tom22 and in the membrane dependent on assembly into the complex with Tom40. be that the in these components not to a in import that be in mitochondria, mitochondrial proteins were at levels is that the reduced growth of the the at which mitochondrial proteins be imported that their levels not from wild type is supported by the that import of mitochondrial precursors into isolated mitochondria reduced mitochondria have reduced ability to import mitochondrial precursor Mitochondria were isolated from the and growth in and that mitochondria in contained reduced levels of Tom40. Import of precursors the of the the mitochondrial and the at for the a with to mitochondria were and to The were to and to The contained of the in import The precursor and forms of and are from treated with to import to that import the of mitochondria, of the protein by growth in were by Mitochondria with reduced levels of Tom40 were and contained is the and acid residues of Tom40 that are for to or for assembly into the TOM complex. of the protein from the of conserved residues We that a conserved region near the N terminus (residues for assembly of N. into the TOM complex Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google The region is by of residues that are conserved crassa and conserved and these residues were for the assembly of Tom40, of the lacking the residues the residues and the residues from 51–60 These were and in vitro to Tom40 precursor proteins for import into isolated type Tom40 precursor to in a 250-kDa intermediate when imported into isolated mitochondria at Neupert Biol. PubMed Scopus Google Scholar, Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google The model of Tom40 assembly that the precursor further into the 400-kDa TOM complex a 100-kDa intermediate import at N. N. Nat. Biol. 2001; PubMed Scopus Google a reduced to be imported into the assembled TOM complex at and to in the 250-kDa assembly intermediate of the and precursors the assembled suggesting a on assembly. the and of assembled of import at a of on the of the 100-kDa which not a at when the of Tom40 N-terminal into the TOM complex. a region of the from is to the and residues in the Tom40 and residues are by the changed from a to an Ala in the are in the to precursors of a wild type Tom40 and the were at or with wild type mitochondria for Mitochondria were and in containing The were on blue native to and analyzed by The of the 400-kDa TOM complex and the and 250-kDa intermediates are Tom40 growth of from a and a were into containing with at and at the of N-terminal Mitochondria were isolated from a and strains expressing the Tom40 or The were with or and by The gel to membrane and with to Tom40. The of is on Mitochondria from and a mutant were with gel and to The gel to and with to Tom40 and of mutant were to of containing the and forms of Tom40 reduced growth and an to the of growth the that of the assembled into the TOM complex in the of assembly in must be to strains expressing of Tom40 were growth in the strains were and were at where the strains at the of The strains the strains containing the the of assembly of these Tom40 that in vitro with the of in In when analyzed by the TOM complex in of the strains to be in when mitochondria are with and into a of of Tom40 in the containing mitochondria from the mitochondria from were in in the of Tom40 to the of Tom40 may have to of the complex from in an to the the of the N-terminal region on Tom40 a of residues in the region of the in Mutant of N. crassa in which the residues at 321–323 were deleted or changed to Ala residues were The were and in vitro to mutant precursor proteins for in import The import and assembly of the precursor to the wild type assembly to the 400-kDa complex the the not progress to the 250-kDa intermediate import at and not the assembled complex at the of the residues the ability of Tom40 precursors to assemble into the TOM whereas the residues to In with the assembly in were to the tom40 with containing the the strains with growth were isolated of mitochondria isolated from strains revealed in TOM complex stability in the a of Tom40 not in the 400-kDa assembled form and at a that to a Tom40 these is to the form of the complex forms and or in of mitochondria containing the Tom40 in in Tom40 a We have that the in Tom40 proteins (residues of crassa is not required for assembly Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google or of the TOM complex. and TOM complex containing the lacking (residues from in of TOM complex stability on blue native of the complex is not by of the protein at the C The role of residues 321–323 in the and stability of the TOM complex further demonstrated by the that mitochondria containing the imported mitochondrial precursors mitochondria We a on blue native of Tom40 import that not in previous We the to be in The not in when import at the 250-kDa and the of the import where Tom40 precursor for a at The of precursor assembly were then a of at The showed that the of the form not the of the the Tom40 precursor in a showed the the and 250-kDa intermediates and the assembled 400-kDa the of Tom40 precursor in the intermediates in the 400-kDa form the levels of in the intermediates were for could not that the of Tom40 precursor in the 250-kDa form in the 100-kDa intermediate N. N. Nat. Biol. 2001; PubMed Scopus Google In the Tom40 precursor in intermediates The of of the precursor from Tom40 assembled to the 400-kDa to the of the intermediates by the of import to or and the to reduced the of assembly but revealed in precursor of import and assembly of mutant Tom40 precursors the that the 250-kDa intermediate is to the 100-kDa form on the of sodium that a imported Tom40 precursor in the 250-kDa intermediate is with the mitochondrial outer membrane in the the when the precursor to the 100-kDa intermediate and the 400-kDa assembled an membrane protein N. N. Nat. Biol. 2001; PubMed Scopus Google We to the of Tom40 precursor in the 250-kDa intermediate and that the of the intermediate form reduced of at the of these not that imported Tom40, which at intermediate when import is at assembled into the 400-kDa form of the TOM complex a of is in where the of Tom40 precursor in the 250-kDa form import at in the and of the assembled 400-kDa complex of import with when import at when of the imported precursor in the assembled form mitochondria were to of the precursor imported at in the assembled complex The that further assembly to the 400-kDa form a of the at with sodium for the the were in an for the of These that assembly of precursors into the 400-kDa form is by the of the of Tom40 precursor from the 250-kDa the that Tom40 in the intermediate may have assembled into the 400-kDa form the be that the imported Tom40 in the 400-kDa complex not assembled Tom40. treated with which to and products when the protein is assembled Neupert Biol. PubMed Scopus Google Scholar, Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google These be in not treated with sodium The of these are reduced in and the is a of is Tom40 in the membrane created by the action of is to the and Tom40 in We that the in the 400-kDa form that by the action of assembled Tom40. The precursor of the Tom40 at the 250-kDa intermediate import at and We to the protein arrested at assemble into the 400-kDa complex the of in the mutant form at the 250-kDa of import at the wild type precursor at the not to the assembled form in the presence of sodium and a of the protein in the intermediate and a precursor that is at the 250-kDa is of the in the 250-kDa intermediate suggesting that at of the imported Tom40 molecules at the 250-kDa are into the membrane. may be to the 100-kDa form the in the near in to the The 100-kDa form to have a when the Tom40 precursor forms of that Tom40 precursor in the 250-kDa form is with in the precursor form of the Tom40. is from the 250-kDa intermediate with and is not to the assembled form and of the in to or a not of the 250-kDa intermediate or the 400-kDa assembled form in is that of Tom40 the 100-kDa intermediate that the form of Tom40 is of the 250-kDa intermediate of the assembly assembly mutants that at the 250-kDa intermediate that the Tom40 precursor a with the membrane at on the assembly of the and mutant of Tom40 showed that these forms of the protein at the 250-kDa intermediate of the a in the region from Tom40 to the 100-kDa form is the assembly of these mutants and to the 100-kDa form in the import of wild type precursor is These the that of the 250-kDa form the of the 100-kDa of to Tom40 precursors be into mitochondria with TOM complex containing mutant of Tom40. type Tom40 precursor proteins were imported into mitochondria isolated from a by of the of with the of Tom40 Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google The TOM complex in these mitochondria the mutant of the Surprisingly, wild type Tom40 precursors in a form of when imported into mitochondria of the mutant at not to the at that by the and in A. of precursor in the 250-kDa but the 100-kDa form not import for at assembly to the 400-kDa form but the intermediates were of the wild type precursor to the assembled form a of of import into the of the 250-kDa intermediate but a for the 100-kDa intermediate not at point The of precursor molecules in the intermediate to the 400-kDa form in a that is with a precursor to showed that Tom40 precursor from the but not the assembled form with import into wild type mitochondria, at of the Tom40 precursor into the assembled 400-kDa form the of with demonstrated that Tom40 not assembled in in the intermediate that the form at but in the correct in the 400-kDa form at by the of the and These that the assembly pathway of Tom40 precursor by the N-terminal of Tom40 molecules in the TOM complex of the mutant Tom40 to be essential for the viability and reduced levels of Tom40 in the of mitochondrial precursors in the cytosol A. PubMed Scopus Google We have these by that tom40 is an essential gene in N. crassa and that mitochondria containing reduced levels of Tom40 are deficient in their to import precursor proteins in We have the by that mitochondria with levels of Tom40 are and are of is that growth and of mitochondria are by the of Tom40 and that the in growth of with levels of the protein is to the reduced to essential in the mitochondria are in growing deficient in components of the TOM complex and Tom22 A. Neupert PubMed Scopus Google Scholar, Neupert Biol. PubMed Scopus Google Mitochondria deficient in Tom40 have reduced levels of the TOM complex components Tom22 and These are to the to import and/or assemble the proteins in the of Tom40. The that reduced levels of Tom40 reduced of these by that the for Tom22 is at We have that a conserved region near the N terminus of Tom40 in TOM complex assembly Neupert Mol. Biol. Cell. 2001; PubMed Scopus Google The lacking residues 40–48 of the N. crassa Tom40 at into the complex wild type Tom40 that an region The mutant form of Tom40 is to progress the 250-kDa intermediate to the assembled TOM complex of import at The of residues 51–60 not assembly in strains expressing form of the protein are growth and in TOM complex the region by the and plays an role for the interactions for the 250-kDa intermediate on the assembly The of assembly to intermediate of the at the protein may not be in an the precursor be imported to the 250-kDa intermediate but to the membrane of the assembly The of the assembly in vitro are supported by the that a tom40 gene a the tom40 that Tom40 must be in a for into the membrane Neupert Biol. PubMed Scopus Google and the may be to the correct for that are in at the protein the recognition and the 250-kDa intermediate in The residues a for into the membrane or assembly with TOM complex but the residues to on in vitro assembly and gene the the strains have growth and TOM complex defects. is that the residues form of a In a for the of the and could be that with residues the region to the whereas of the residues not membrane and a region be for near the C terminus and the of the TOM complex from the is that the region could be in interactions TOM complex The presence of the Tom40 complex in is of the of Tom40 in S. A. N. PubMed Scopus Google the Tom40 mutant have interactions with The of the complex in mitochondria to Tom40 with that the region could to the and of Tom40 that Tom40 precursor in the 250-kDa intermediate to the 100-kDa form on the assembly pathway N. N. Nat. Biol. 2001; PubMed Scopus Google We were to in wild type Tom40 forms and the assembly of mutant Tom40 molecules to the and the 100-kDa intermediates be the import of wild type and mutant forms of the that a on the assembly the of the 250-kDa form with of the 100-kDa intermediate in the and the that the Tom40 precursor in the 250-kDa form and then to the 100-kDa form. that the Tom40 precursor in the 250-kDa intermediate is with the outer membrane on the and is with sodium N. N. Nat. Biol. 2001; PubMed Scopus Google from of mitochondria import of wild type Tom40 into wild type mitochondria not of of the model to the that assembly of Tom40 precursors in intermediates into the 400-kDa form. the that precursors of the and of Tom40 in the 250-kDa intermediate were by the that the Tom40 precursor is with the membrane at for the action of sodium on wild type precursors be that protein-protein interactions the at an intermediate of and these are in the presence of is that interactions Tom40 molecules in TOM may be of with incoming molecules. Analysis of the import and assembly of wild type Tom40 precursors into mitochondria containing the mutant form of Tom40 revealed from the assembly of the precursor in the 250-kDa and in the 100-kDa form. the precursor in a which to assemble into the 400-kDa form. The for the form is that a precursor with an TOM complex. Most of the precursor at with sodium that with the components in the form must into the membrane. is of the 100-kDa the precursor may into the TOM by a pre-existing that acid residues 40–48 of Tom40 molecules in the TOM complex may with incoming may be that an alternate pathway is that a of assembly by pathway but is not the N terminus of Tom40 is not required for interactions Tom40 molecules 2001; PubMed Google that the region is for assembly of the protein into the TOM in the N terminus of Tom40 precursors and Tom40 molecules in the TOM complex have an on the assembly We are to and for and to for on the

Récupéré en direct depuis OpenAlex et désinversé. Les résumés ne sont pas conservés dans cette base de données : les index inversés représentent 8,6 Go des 9,3 Go de texte de la base, et le serveur dispose de 13 Go libres.