Domain Swapping Localizes the Structural Determinants of Regioselectivity in Membrane-bound Fatty Acid Desaturases of Caenorhabditis elegans

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Nature

Retraction

Reason

Misconduct by Author;

Date

6/23/2006 0:00

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Abstract

Most fatty acid desaturases are members of a large superfamily of integral membrane, O2-dependent, ironcontaining enzymes that catalyze a variety of oxidative modifications to lipids. Sharing a similar primary structure and membrane topology, these enzymes are broadly categorized according to their positional specificity or regioselectivity, which designates the preferred position for substrate modification. To investigate the structural basis of regioselectivity in membrane-bound desaturases, the Caenorhabditis elegans ω-3 (FAT-1) and “Δ12” (FAT-2) desaturases were used as a model system. With the use of unnatural substrates, the regioselectivity of C. elegans FAT-2 was clearly defined as ν+3, i.e. it “measures” three carbons from an existing double bond. The structural basis for ν+3 and ω-3 regioselectivities was examined through construction and expression of chimeric DNA sequences based on FAT-1 and FAT-2. Each sequence was divided into seven domains, and chimeras were constructed in which specific domains were replaced with sequence from the other desaturase. When tested by expression in yeast using exogenously supplied substrates, chimeric sequences were found in which domain swapping resulted in a change of regioselectivity from ν+3to ω-3 and vice versa. In this way, the structural determinants of regioselectivity in FAT-1 and FAT-2 have been localized to two interdependent regions: a relatively hydrophobic region between the first two histidine boxes and the carboxyl-terminal region. Most fatty acid desaturases are members of a large superfamily of integral membrane, O2-dependent, ironcontaining enzymes that catalyze a variety of oxidative modifications to lipids. Sharing a similar primary structure and membrane topology, these enzymes are broadly categorized according to their positional specificity or regioselectivity, which designates the preferred position for substrate modification. To investigate the structural basis of regioselectivity in membrane-bound desaturases, the Caenorhabditis elegans ω-3 (FAT-1) and “Δ12” (FAT-2) desaturases were used as a model system. With the use of unnatural substrates, the regioselectivity of C. elegans FAT-2 was clearly defined as ν+3, i.e. it “measures” three carbons from an existing double bond. The structural basis for ν+3 and ω-3 regioselectivities was examined through construction and expression of chimeric DNA sequences based on FAT-1 and FAT-2. Each sequence was divided into seven domains, and chimeras were constructed in which specific domains were replaced with sequence from the other desaturase. When tested by expression in yeast using exogenously supplied substrates, chimeric sequences were found in which domain swapping resulted in a change of regioselectivity from ν+3to ω-3 and vice versa. In this way, the structural determinants of regioselectivity in FAT-1 and FAT-2 have been localized to two interdependent regions: a relatively hydrophobic region between the first two histidine boxes and the carboxyl-terminal region. Retraction: Domain swapping localizes the structural determinants of regioselectivity in membrane-bound fatty acid desaturases of Caenorhabditis elegans. VOLUME 279 (2004) PAGES 39296-39302Journal of Biological ChemistryVol. 281Issue 25PreviewThe authors have retracted this paper in its entirety based on the admission of scientific misconduct on the sole part of the first author. Full-Text PDF Open Access Fatty acid desaturases are part of multicomponent systems that catalyze the oxygen-and nicotinamide adenine dinucleotide-dependent syn-dehydrogenation of unactivated aliphatic regions of their fatty ester (acyl-lipid) or thioester (acyl-acyl carrier protein or acyl-CoA) substrates (1Buist P.H. Nat. Prod. Rep. 2004; 21: 249-262Crossref PubMed Scopus (96) Google Scholar, 2Behrouzian B. Buist P.H. Prostaglandins Leukot. Essent. Fatty Acids. 2003; 68: 107-112Abstract Full Text Full Text PDF PubMed Scopus (48) Google Scholar, 3Sperling P. Ternes P. Zank T.K. Heinz E. Prostaglandins Leukot. Essent. Fatty Acids. 2003; 68: 73-95Abstract Full Text Full Text PDF PubMed Scopus (241) Google Scholar, 4Los D.A. Murata N. Biochim. Biophys. Acta. 1998; 1394: 3-15Crossref PubMed Scopus (441) Google Scholar, 5Shanklin J. Cahoon E.B. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1998; 49: 611-641Crossref PubMed Scopus (731) Google Scholar, 6Heinz E. Moore Jr., T.S. Lipid Metabolism in Plants. CRC Press, Boca Raton, FL1993: 33-89Google Scholar). In addition to the family of soluble fatty acid desaturases, of which the plant stearoyl-acyl carrier protein desaturase is well characterized, there is a large group of structurally distinct integral membrane desaturases. Membrane desaturases of widely varying substrate specificity and regioselectivity are scattered among a range of taxa. The yeast Saccharomyces cerevisiae has a single stearoyl-CoA Δ9 desaturase, whereas many bacteria lack such desaturases entirely. At the other extreme, the biosynthesis of (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoic acid in some marine fungi likely requires the successive action of six structurally similar membrane desaturases, each varying in substrate specificity and regioselectivity (7Qiu X. Hong H. MacKenzie S.L. J. Biol. Chem. 2001; 276: 31561-31566Abstract Full Text Full Text PDF PubMed Scopus (194) Google Scholar, 8Qiu X. Prostaglandins Leukot. Essent. Fatty Acids. 2003; 68: 181-186Abstract Full Text Full Text PDF PubMed Scopus (118) Google Scholar). Based on structural and catalytic similarities, membrane desaturases are included in a superfamily of oxidative enzymes along with alkane hydroxylase, xylene monooxygenase, carotene ketolase, and sterol methyloxidase (9Shanklin J. Whittle E. Fox B.G. Biochemistry. 1994; 33: 12787-12794Crossref PubMed Scopus (650) Google Scholar, 10Shanklin J. Whittle E. FEBS Lett. 2003; 545: 188-192Crossref PubMed Scopus (58) Google Scholar). These are thought to contain a histidine-coordinated diiron center at the active site. While essentially no three-dimensional structural information is available for these difficult to purify enzymes, primary structure similarity, especially the conservation of three histidine-rich motifs, and similarity of hydrophobicity patterns support their structural similarity. On this basis, a model for the membrane topology of this superfamily has been proposed as depicted in Fig. 1 (9Shanklin J. Whittle E. Fox B.G. Biochemistry. 1994; 33: 12787-12794Crossref PubMed Scopus (650) Google Scholar, 11Stukey J.E. McDonough V.M. Martin C.E. J. Biol. Chem. 1990; 265: 20144-20149Abstract Full Text PDF PubMed Google Scholar, 12van Beilen J.B. Penninga D. Witholt B. J. Biol. Chem. 1992; 267: 9194-9201Abstract Full Text PDF PubMed Google Scholar), although an alternative topology has been suggested (13Diaz A.R. Mansilla M.C. Vila A.J. de Mendoza D. J. Biol. Chem. 2002; 277: 48099-48106Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar). In addition to their oxidative prowess, fatty acid desaturases are remarkable in their individual positional specificity (3Sperling P. Ternes P. Zank T.K. Heinz E. Prostaglandins Leukot. Essent. Fatty Acids. 2003; 68: 73-95Abstract Full Text Full Text PDF PubMed Scopus (241) Google Scholar). Separate desaturases have the ability to introduce a double bond at positions ranging from three carbons from the carboxyl to three carbons from the methyl terminus of fatty acyl substrates. This represents as much as 20 Å in the span of regioselectivity for these enzymes for flexible substrates with few distinguishing functional group landmarks. In fact, the substrate structural references that determine membrane desaturase regioselectivity are relatively complex (6Heinz E. Moore Jr., T.S. Lipid Metabolism in Plants. CRC Press, Boca Raton, FL1993: 33-89Google Scholar). There appear to be three modes of regioselectivity. The Δx desaturases introduce a double bond between Cx and C(x+1) in the fatty acid moiety of the substrate. The ω-x desaturases reference the methyl end of the substrate introducing a double bond between the ω-x and ω-(x-1) positions. There is a third mode of regioselectivity called ν+x in which the double bond is introduced relative to an existing double bond. An example of this is the so-called extraplastidial “Δ12” 1While not strictly correct, the Δ12 nomenclature is retained and used in quotation marks in this paper to comply with historical usage. desaturase of plants. The natural substrate of the enzyme is oleoyl phosphatidylcholine, which it converts to linoleoylphosphatidylcholine. However, the enzyme will also desaturate 19:1(10) 2The abbreviations used are: X:Y(m,n,...), a fatty acid containing X carbons with Y cis double bonds at positions m,n,..., counted from the carboxyl terminus; GC, gas chromatography; HPLC, high performance liquid chromatography; MS, mass spectrometry. to 19:2(10,13) suggesting a regioselectivity that yields a double bond that is three carbon atoms distal to an existing double bond within a limited range relative to the carboxyl terminus (6Heinz E. Moore Jr., T.S. Lipid Metabolism in Plants. CRC Press, Boca Raton, FL1993: 33-89Google Scholar, 14Schwartzbeck J.L. Jung S. Abbott A.G. Mosley E. Lewis S. Pries G.L. Powell G.L. Phytochemistry (Oxf.). 2001; 57: 643-652Crossref PubMed Scopus (40) Google Scholar). The recently discovered Δ5/Δ6 desaturase of zebrafish apparently represents a ν-3 desaturase (15Hastings N. Agaba M. Tocher D.R. Leaver M.J. Dick J.R. Sargent J.R. Teale A.J. Proc. Natl. Acad. Sci. U. S. A. 2001; 98: 14304-14309Crossref PubMed Scopus (282) Google Scholar) in that it references double bonds at the Δ8 and Δ9 positions. Given the nutritional and commercial importance of unsaturated fatty acids of various types (16Roche H.M. Proc. Nutr. Soc. 1999; 58: 397-401Crossref PubMed Scopus (95) Google Scholar), it is essential that we develop an understanding of the structure-function relationships of integral membrane fatty acid desaturases. Integral membrane proteins are notoriously difficult to study in vitro. Given this, we have undertaken a study of the structural determinants of desaturase regioselectivity through the use of domain swapping experiments coupled with heterologous expression in yeast. The “Δ12” (FAT-2) and ω-3 (FAT-1) fatty acid desaturases from the nematode Caenorhabditis elegans were used as a model system. These enzymes are involved in the biosynthesis of polyunsaturated fatty acids in C. elegans that range from 18:2(9,12) to 20:5(5,8,11,14,17) (17Watts J.L. Browse J. Proc. Natl. Acad. Sci. U. S. A. 2002; 99: 5854-5859Crossref PubMed Scopus (309) Google Scholar, 18Peyou-Ndi M.M. Watts J.L. Browse J. Arch. Biochem. Biophys. 2000; 376: 399-408Crossref PubMed Scopus (87) Google Scholar, 19Spychalla J.P. Kinney A.J. Browse J. Proc. Natl. Acad. Sci. U. S. A. 1997; 94: 1142-1147Crossref PubMed Scopus (187) Google Scholar, 20Napier J.A. Michaelson L.V. Lipids. 2001; 36: 761-766Crossref PubMed Scopus (42) Google Scholar). The two enzymes share 51% amino acid sequence identity. As such, they are two of the most similar desaturases, which differ distinctly in regioselectivity and especially regioselective mode (3Sperling P. Ternes P. Zank T.K. Heinz E. Prostaglandins Leukot. Essent. Fatty Acids. 2003; 68: 73-95Abstract Full Text Full Text PDF PubMed Scopus (241) Google Scholar), the manner in which the position of the incipient double bond is determined. In fact, the precise regioselective mode of the so-called “Δ12” desaturase of C. elegans (FAT-2) has not been determined previously. Here we report characterization of the regioselectivity of FAT-2 and the use of domain swapping experiments in an attempt to localize the structural determinants of regioselectivity in membrane-bound fatty acid desaturases. Materials—Fatty acids (typically >99% purity) were purchased from Nu-Chek Prep, Inc. (Elysian, MN). Tergitol (type Nonidet P-40) was obtained from Sigma. Preparation of fat-1 and fat-2 Constructs—A construct containing the C. elegans fat-1 gene was obtained by PCR-amplifying the sequence from plasmid pDM015 (21Meesapyodsuk D. Reed D.W. Savile C.K. Buist P.H. Ambrose S.J. Covello P.S. Biochemistry. 2000; 39: 11948-11954Crossref PubMed Scopus (68) Google Scholar) using oligonucleotide primers fat-1start and fat-1end (Table I). The resulting fragment was gel-purified and cloned into vector pYES2.1/V5-His-TOPO (Invitrogen) to yield plasmid pSAS001 suitable for the expression of the FAT-1 enzyme in S. primers used to construct chimeras of C. elegans ω-3 and “Δ12” fatty acid Open in a The of fat-2 was cloned into the vector pYES2.1/V5-His-TOPO to yield plasmid as D.W. D.R. Buist P.H. Ambrose S.J. Savile C.K. A.R. Covello P.S. J. Chem. Soc. 2003; PubMed Scopus Google Scholar). To in a has been introduced into the sequence D.W. D.R. Buist P.H. Ambrose S.J. Savile C.K. A.R. Covello P.S. J. Chem. Soc. 2003; PubMed Scopus Google Scholar). of for construction were the pSAS001 and containing fat-1 and fat-2 DNA sequences from were using the C. 1998; PubMed Scopus Google Scholar). of the and primers used in the construction of chimeras are in The primers sequence from desaturase and were used to to specific regions of of the desaturases. from these as in a The sequence at the of the to the other desaturase and of the using a which was using the primers or and or The for a was for for for 1 for of for The for a was for for 1 for 1 for 1 for were from a and cloned into the yeast expression vector pYES2.1/V5-His-TOPO the The of chimeric was by DNA and cerevisiae was with each construct using the S. C. (Invitrogen) with on of desaturase yeast were to in for at on and with Moore J.A. in Scholar). yeast containing the plasmid vector was used as a In some fatty acids were to a of with Tergitol (type Nonidet 1 and were using a from were in at for and by on were by with or to for were with and 20 in and with primary this, from a with a to amino acid sequence by FAT-1 acids and FAT-2 acids to was the primary the membrane was with containing 20 and with and by using Fatty of fatty acid methyl was as D.W. D.R. Buist P.H. Ambrose S.J. Savile C.K. A.R. Covello P.S. J. Chem. Soc. 2003; PubMed Scopus Google Scholar). fatty acid methyl of were from the fatty acid methyl ester by using an with the from in and using a at with to in 20 The containing the fatty acids of were (21Meesapyodsuk D. Reed D.W. Savile C.K. Buist P.H. Ambrose S.J. Covello P.S. Biochemistry. 2000; 39: 11948-11954Crossref PubMed Scopus (68) Google Scholar) and to according to and C. Scopus Google Scholar). The were by the to a with of and the with of The was a and the were in of for of the was using an mass coupled to an gas using and and with a with The included a the using a of an of for 1 and a of to The mass was an range of at of the C. elegans “Δ12” the regioselective mode of yeast were in with available fatty The use of and 19:1(10) as substrates and of the FAT-2 the between the and ν+3 types of regioselectivity. The fatty acid of the was by and with yeast an plasmid in and of fatty acids from the with exogenously or 19:1(10) not in the vector In the of supplied with the with and was by of the as the ν+3 and Fig. a mass of the The at mass and the at and are with double bonds at the and positions. The for the 19:1(10) is also with double bonds at the and positions not The double bond are by patterns that are with 18:2(9,12) and obtained the not the of 19:1(10) was found to be to the for which fatty acids not The that by FAT-2 not at the Δ12 position for and of the integral membrane fatty acid desaturases are thought to share the membrane topology and three-dimensional structure A.R. Mansilla M.C. Vila A.J. de Mendoza D. J. Biol. Chem. 2002; 277: 48099-48106Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar). This is of C. elegans FAT-1 and FAT-2 they share 51% amino acid sequence identity. in amino acid sequence domains of of these enzymes with the domains from the other we at in some to this topology and structure as well as desaturase With this in we to investigate the structural that determine regioselectivity in the two enzymes through domain swapping for construction were on a structural basis as the 1994; Google Scholar) to the of the in FAT-1 and a membrane model was constructed based on (9Shanklin J. Whittle E. Fox B.G. Biochemistry. 1994; 33: 12787-12794Crossref PubMed Scopus (650) Google Scholar, 11Stukey J.E. McDonough V.M. Martin C.E. J. Biol. Chem. 1990; 265: 20144-20149Abstract Full Text PDF PubMed Google Scholar, 12van Beilen J.B. Penninga D. Witholt B. J. Biol. Chem. 1992; 267: 9194-9201Abstract Full Text PDF PubMed Google Scholar) chimeric sequence were in the the sequence was to the membrane on the were the histidine and was the third histidine These the desaturases into seven structural the region acids FAT-1 the first of acids the boxes and and an relatively hydrophobic acids a relatively hydrophobic acids the of acids a relatively domain containing acids and the carboxyl-terminal region acids Fig. chimeras from introducing single and domains from the desaturase. are according to the of the sequence and the of the domain introduced from the other a of FAT-1 sequence with domain replaced by domain from FAT-2. of the various and chimeric fatty acid desaturases were determined by as in Fig. the most within a group of desaturase protein in yeast were similar or with the for single domain chimeras with an ω-3 it is from Fig. that expression were of the and is no with a “Δ12” a range of expression with and relative to FAT-2 and the other the with the domain was at to the The double domain enzymes were at that were or with the and Given the expression it was to and the of the various enzymes in yeast of Domain is an for heterologous expression in the study of membrane-bound desaturases and enzymes P.S. Reed D.W. Plant Physiol. PubMed Scopus Google Scholar). the polyunsaturated of the ω-3 and “Δ12” desaturases are not the of in the be used as a of enzyme (21Meesapyodsuk D. Reed D.W. Savile C.K. Buist P.H. Ambrose S.J. Covello P.S. Biochemistry. 2000; 39: 11948-11954Crossref PubMed Scopus (68) Google Scholar, D.W. Covello P.S. Plant Physiol. 2000; PubMed Scopus Google Scholar). functional the and chimeric enzymes were in the S. cerevisiae supplied with various fatty acid substrates, and the yeast were for fatty acid As a yeast was also with the plasmid were constructed as to to amino acid sequences with the of a in FAT-2 that with sequences D.W. D.R. Buist P.H. Ambrose S.J. Savile C.K. A.R. Covello P.S. J. Chem. Soc. 2003; PubMed Scopus Google Scholar, M. J. Biol. PubMed Scopus Google Scholar). The fatty acid desaturase of the single domain chimeras are in Fig. chimeras containing a single domain were active and retained the regioselectivity of their desaturase. of the ω-3 chimeras ν+3 with or not as well as that of ω-3 the ω-3 desaturase on the substrates 18:2(9,12) and and the However, there are some in relative for the two substrates. FAT-1 from 18:2(9,12) from most chimeras from each substrate with the of which to have a for In and that were to or the ω-3 The other ω-3 chimeras with single domains from FAT-2 sequence relative to The was most of of with substrates. from the chimeras containing single domains the importance of domain The through chimeras on that is to that of the “Δ12” desaturase. On the other 18:2(9,12) in yeast was of chimeras a of relative to with the the most ω-3 on 18:2(9,12) was for the chimeras containing single domains not of Domain of the single domain chimeras that the structure by single domain be for the of regioselectivity. However, these a to be is of that the domains from each desaturase support enzyme at in the we that the for in and chimeras be a of essential structural or functional in the enzyme between domain and other such be be along with on regioselectivity. On this basis, a of chimeras was constructed that domain and of the other six domains from the desaturase The of these chimeras were on a variety of substrates and and fatty acid of of yeast these chimeras were from the not However, two chimeric sequences were discovered in which domain swapping resulted in a change of regioselectivity from ν+3 to ω-3 and vice versa. When domains and were replaced with sequence from the other desaturase, the resulting regioselectivity with the that resulting from the expression of is with FAT-1 in Fig. the was found to the fatty acid substrates 18:2(9,12) and into ω-3 at to that of yeast expression of the in yeast resulted in the of 18:2(9,12) from Fig. the structure of the and domains not determine positional the of the two domains from of desaturase is to determine the regioselectivity of the chimeric There is structure-function relationships for the superfamily of integral membrane which most fatty acid desaturases. and are with histidine-rich of a diiron center at the active of these enzymes J. Whittle E. FEBS Lett. 2003; 545: 188-192Crossref PubMed Scopus (58) Google Scholar, J. C. H. Fox B.G. E. Proc. Natl. Acad. Sci. U. S. A. 1997; 94: PubMed Scopus Google Scholar). histidine have been to be for with the of that is replaced by in some desaturases, which introduce double bonds in the substrate (3Sperling P. Ternes P. Zank T.K. Heinz E. Prostaglandins Leukot. Essent. Fatty Acids. 2003; 68: 73-95Abstract Full Text Full Text PDF PubMed Scopus (241) Google Scholar, B. A. J.A. J. 2001; PubMed Scopus Google Scholar). and J.A. Whittle E. J. J. Biol. Chem. 2002; 277: Full Text Full Text PDF PubMed Scopus Google Scholar) have a of individual amino acids that are for the of the enzymes, which to have desaturase and to varying domain swapping study was undertaken by and B. Michaelson L.V. Lewis M.J. J.A. Biochem. Biophys. 2000; PubMed Scopus Google Scholar) to investigate the regioselectivity and substrate specificity of two desaturases. This at the importance of the carboxyl terminus of desaturases in specific substrate of these the of a carboxyl-terminal of the desaturase the importance of domain in desaturase (13Diaz A.R. Mansilla M.C. Vila A.J. de Mendoza D. J. Biol. Chem. 2002; 277: 48099-48106Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar). In this two desaturases were that have a high of sequence similarity. While the substrate of FAT-1 and FAT-2 are not it has been suggested that they are desaturases M.M. Watts J.L. Browse J. Arch. Biochem. Biophys. 2000; 376: 399-408Crossref PubMed Scopus (87) Google Scholar). natural substrates are similar in and have double bonds at is the position of the incipient double i.e. the “Δ12” desaturase on a Δ9 and the ω-3 desaturase on substrates. However, the enzymes differ in regioselectivity and regioselective FAT-2 “measures” from a double bond by its on and and FAT-1 from the methyl end of the substrate. The ν+3 regioselectivity of FAT-2 determined by this study is similar to that found for the plant desaturase J.L. Jung S. Abbott A.G. Mosley E. Lewis S. Pries G.L. Powell G.L. Phytochemistry (Oxf.). 2001; 57: 643-652Crossref PubMed Scopus (40) Google Scholar). to the structural determinants of desaturase regioselectivity was to construct single domain chimeric enzymes in which domain in a enzyme was replaced with the domain sequence of the other is to the of a example of such a chimeric be be active and the regioselectivity of the desaturase, suggesting that the domain is not for regioselectivity. The regioselectivity to that of the introduced suggesting that it is the of positional are that the chimeric enzyme have regioselectivities or a regioselectivity such as for In the for the C. elegans FAT-1 and single domain chimeras of enzymes with of positional The to be from this is that no single domain is or to regioselectivity on the This the that two or domains in to determine regioselectivity. In the of a of we to the single domain that that domain was and a domain in of between the two Most of the chimeras were there are to the of most The chimeras in which and were regioselectivities to the of the and domains, i.e. and domains to the ω-3 these two domains appear to be in large part to the of regioselectivity in the ω-3 and “Δ12” desaturases of C. elegans. The importance of domain in C. elegans desaturase is with that or of sequence at the carboxyl terminus of desaturases (13Diaz A.R. Mansilla M.C. Vila A.J. de Mendoza D. J. Biol. Chem. 2002; 277: 48099-48106Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar). The from on C. elegans desaturases this to that the carboxyl terminus is an of regioselectivity. Domain is for regioselectivity and substrate of this relatively hydrophobic region the histidine in the FAT-1 the relative on This and its importance in regioselectivity that domain be involved in and of the substrate relative to the active site. is that of the domains are in the of regioselectivity and that and domains are thought to be on the of the While domain the active histidine domain is to the and domain is to the third of of domains and for FAT-1 and FAT-2 a of amino acid is in to the amino acid that are for regioselectivity. Browse for a of C. elegans the Plant DNA for and and for of the

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The record

Venue

Journal of Biological Chemistry

Topic

Lipid metabolism and biosynthesis

Field

Biochemistry, Genetics and Molecular Biology

Canadian institutions

Plant Biotechnology Institute

Funders

Natural Sciences and Engineering Research Council of Canada

Keywords

RegioselectivityCaenorhabditis elegansBiochemistryChemistryStereochemistryBiologyGene

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