Analysis of acyltransferases in Caenorhabditis elegans Export

@inproceedings{citeulike:3284882, abstract = {In the biosynthesis of phospholipids and triacylglycerol, glycerol phosphate is sequentially acylated at the sn -1 and sn -2 positions by acyltransferases, namely by glycerol-3-phosphate acyltransferase (GPAT) and lysophosphatidic acid acyltransferase (LPAAT). Both GPAT and LPAAT have been reported to contain highly conserved regions consisting of four repetitive blocks of the so-called acyltransferase motif. A human genome database search revealed 15 genes containing the acyltransferase motif, of which physiological functions and substrate specificities are largely unknown. In this study, we identified 14 genes containing the acyltransferase motif in C. elegans genome sequences ( acl-1 \~{} 14 ), and focused on acl-4 , which shows a significant homology with the corresponding human genes. To elucidate the physiological functions of acl-4 , we isolated the deletion mutants by UV/TMP method. The acl-4 (qa3110) allele contains a premature stop mutation predicted to delete acyltransferase motif, suggesting that this allele is likely to eliminate gene function completely. The acl-4 (qa3110) grew normally and exhibited no apparent abnormal phenotype. Since acl genes encode the putative acyltransferases, which transfer fatty acyl chain to the lysophospholipid, we analyzed the acl-4 (qa3110) in fat mutant backgrounds in which fatty acid compositions are altered (Watts et al ., 2002 PNAS 99 , 5854-5859, Lesa et al ., 2003 J Cell Sci. 116 , 4965-4975). Interestingly, we found that acl-4;fat-3 double mutants, which are depleted of long chain polyunsaturated fatty acids(LC-PUFAs), showed severe movement abnormalities. These defects were rescued by application of exogenous LC-PUFAs. Next, we examined the expression pattern of acl-4 . We generated transgenic worms expressing acl-4p::GFP and found that acl-4p::GFP was expressed in ventral nerve cord, some sensory neurons and muscles. We are currently trying to rescue the movement defects of the acl-4;fat-3 mutants by the tissue specific fat-3 expression, and to examine the substrate specificity in vitro .}, author = {Hara, Naoko and Inoue, Takao and Takanezawa, Yasukazu and Arai, Hiroyuki}, citeulike-article-id = {3284882}, citeulike-linkout-0 = {http://www.wormbase.org/db/misc/paper?name=WBPaper00010050}, journal = {East Asia Worm Meeting}, keywords = {acl-1, acl-4, c\_elegans, caenorhabditis\_elegans, celegans, elegans, f49h126, f59f44, fat-3, meeting\_abstract, nematode, w08d24, wormbase}, posted-at = {2008-09-18 09:13:37}, priority = {3}, title = {Analysis of acyltransferases in Caenorhabditis elegans}, url = {http://www.wormbase.org/db/misc/paper?name=WBPaper00010050}, year = {2004} }

TY - CONF ID - citeulike:3284882 L3 - citeulike-article-id:3284882 N2 - In the biosynthesis of phospholipids and triacylglycerol, glycerol phosphate is sequentially acylated at the sn -1 and sn -2 positions by acyltransferases, namely by glycerol-3-phosphate acyltransferase (GPAT) and lysophosphatidic acid acyltransferase (LPAAT). Both GPAT and LPAAT have been reported to contain highly conserved regions consisting of four repetitive blocks of the so-called acyltransferase motif. A human genome database search revealed 15 genes containing the acyltransferase motif, of which physiological functions and substrate specificities are largely unknown. In this study, we identified 14 genes containing the acyltransferase motif in C. elegans genome sequences ( acl-1 ~ 14 ), and focused on acl-4 , which shows a significant homology with the corresponding human genes. To elucidate the physiological functions of acl-4 , we isolated the deletion mutants by UV/TMP method. The acl-4 (qa3110) allele contains a premature stop mutation predicted to delete acyltransferase motif, suggesting that this allele is likely to eliminate gene function completely. The acl-4 (qa3110) grew normally and exhibited no apparent abnormal phenotype. Since acl genes encode the putative acyltransferases, which transfer fatty acyl chain to the lysophospholipid, we analyzed the acl-4 (qa3110) in fat mutant backgrounds in which fatty acid compositions are altered (Watts et al ., 2002 PNAS 99 , 5854-5859, Lesa et al ., 2003 J Cell Sci. 116 , 4965-4975). Interestingly, we found that acl-4;fat-3 double mutants, which are depleted of long chain polyunsaturated fatty acids(LC-PUFAs), showed severe movement abnormalities. These defects were rescued by application of exogenous LC-PUFAs. Next, we examined the expression pattern of acl-4 . We generated transgenic worms expressing acl-4p::GFP and found that acl-4p::GFP was expressed in ventral nerve cord, some sensory neurons and muscles. We are currently trying to rescue the movement defects of the acl-4;fat-3 mutants by the tissue specific fat-3 expression, and to examine the substrate specificity in vitro . JF - East Asia Worm Meeting TI - Analysis of acyltransferases in Caenorhabditis elegans KW - acl-1 KW - acl-4 KW - c_elegans KW - caenorhabditis_elegans KW - celegans KW - elegans KW - f49h126 KW - f59f44 KW - fat-3 KW - meeting_abstract KW - nematode KW - w08d24 KW - wormbase AU - Hara, Naoko AU - Inoue, Takao AU - Takanezawa, Yasukazu AU - Arai, Hiroyuki PY - 2004/// UR - http://www.wormbase.org/db/misc/paper?name=WBPaper00010050 ER -