Further investigation of the roles of ACN-1, a non-peptidase member of the ACE family, in nematode development. Export

@inproceedings{citeulike:3333907, abstract = { The acn-1 gene of C. elegans is a unique member of the angiotensin-converting enzyme (ACE, M2 metallopeptidase) family that has been shown by RNAi studies to have an essential role in nematode moulting. Interestingly, the central ACE-like domain of ACN-1 lacks conserved active site residues necessary for proteolysis. The N-terminal region of ACN-1 differs substantially from other ACE family members in having a proline/glutamic acid-rich domain, whilst the C-terminal region also contains distinct motifs that include a cysteine-rich region, a mucin-like region and a predicted GPI-anchor attachment site. Homologues of ACN-1 are present in parasitic nematode databases and hence understanding the role of acn-1 in C. elegans development should not only generate new insights into the mechanism of moulting, but potentially, also offer a new target for development of novel anti-nematode agents. We have shown previously using promoter-acn-1-gfp transgenes that acn-1 is expressed strongly prior to each larval moult in hypodermal (hyp7) and seam cells and also that expression occurs in the developing vulva of hermaphrodites and the ray papillae of the male tail. To extend these studies, we have raised ACN-1 specific antibodies against a synthetic peptide sequence and carried out immunocytochemical localisation of the protein in whole nematodes. The data suggests that ACN-1 becomes localised to the cuticle, indicating a possible mechanism for rapid removal of the protein following ecdysis. An acn-1 mutant (tm844), in which a 692 bp fragment of the acn-1 gene has been deleted, has been obtained from the Japanese Gene Knockout Consortium. acn-1 -/- nematodes arrest during embryonic development. We a currently attempting to rescue this lethality by engineering acn-1 constructs that enable us to test the functionality of the various domains within the ACN-1 protein.}, author = {Craig, Hannah L. and Burnham, Susan and Nicol, Clare and Brooks, Darren R. and Isaac, Richard E.}, citeulike-article-id = {3333907}, citeulike-linkout-0 = {http://www.wormbase.org/db/misc/paper?name=WBPaper00030695}, journal = {International Worm Meeting}, keywords = {acn-1, c42d85, c\_elegans, caenorhabditis\_elegans, celegans, elegans, meeting\_abstract, nematode, wormbase}, posted-at = {2008-09-24 21:21:35}, priority = {3}, title = {Further investigation of the roles of ACN-1, a non-peptidase member of the ACE family, in nematode development.}, url = {http://www.wormbase.org/db/misc/paper?name=WBPaper00030695}, year = {2007} }

TY - CONF ID - citeulike:3333907 L3 - citeulike-article-id:3333907 N2 - The acn-1 gene of C. elegans is a unique member of the angiotensin-converting enzyme (ACE, M2 metallopeptidase) family that has been shown by RNAi studies to have an essential role in nematode moulting. Interestingly, the central ACE-like domain of ACN-1 lacks conserved active site residues necessary for proteolysis. The N-terminal region of ACN-1 differs substantially from other ACE family members in having a proline/glutamic acid-rich domain, whilst the C-terminal region also contains distinct motifs that include a cysteine-rich region, a mucin-like region and a predicted GPI-anchor attachment site. Homologues of ACN-1 are present in parasitic nematode databases and hence understanding the role of acn-1 in C. elegans development should not only generate new insights into the mechanism of moulting, but potentially, also offer a new target for development of novel anti-nematode agents. We have shown previously using promoter-acn-1-gfp transgenes that acn-1 is expressed strongly prior to each larval moult in hypodermal (hyp7) and seam cells and also that expression occurs in the developing vulva of hermaphrodites and the ray papillae of the male tail. To extend these studies, we have raised ACN-1 specific antibodies against a synthetic peptide sequence and carried out immunocytochemical localisation of the protein in whole nematodes. The data suggests that ACN-1 becomes localised to the cuticle, indicating a possible mechanism for rapid removal of the protein following ecdysis. An acn-1 mutant (tm844), in which a 692 bp fragment of the acn-1 gene has been deleted, has been obtained from the Japanese Gene Knockout Consortium. acn-1 -/- nematodes arrest during embryonic development. We a currently attempting to rescue this lethality by engineering acn-1 constructs that enable us to test the functionality of the various domains within the ACN-1 protein. JF - International Worm Meeting TI - Further investigation of the roles of ACN-1, a non-peptidase member of the ACE family, in nematode development. KW - acn-1 KW - c42d85 KW - c_elegans KW - caenorhabditis_elegans KW - celegans KW - elegans KW - meeting_abstract KW - nematode KW - wormbase AU - Craig, Hannah AU - Burnham, Susan AU - Nicol, Clare AU - Brooks, Darren AU - Isaac, Richard PY - 2007/// UR - http://www.wormbase.org/db/misc/paper?name=WBPaper00030695 ER -