tailieunhanh - Báo cáo khoa học: A novel carbonic anhydrase from the giant clam Tridacna gigas contains two carbonic anhydrase domains

This report describes the presence of a unique dual domain carbonic anhydrase (CA) in the giant clam,Tridacna gigas. CA plays an important role in the movement of inorganic carbon (Ci ) from the surrounding sea-water to the symbiotic algae that are found within the clam’s tissue. One of these isoforms is a glycoprotein which is significantly larger (70 kDa) than any previously reported from animals (generally between 28 and 52 kDa). | ềFEBS Journal A novel carbonic anhydrase from the giant clam Tridacna gigas contains two carbonic anhydrase domains William Leggat1 2 Ross Dixon1 Said Saleh1 and David Yellowlees1 1 Biochemistry and Molecular Biology James Cook University Townsville Queensland Australia 2 Centre for Marine Studies University of Queensland Queensland Australia Keywords carbonic anhydrase clam symbiosis Correspondence W. Leggat Centre for Marine Studies University of Queensland Queensland 4072 Australia Fax 61 7 33654755 Tel 61 7 33469576 E-mail Notes The nucleotide sequences for carbonic anhydrase from T. gigas have been deposited in the GenBank database under GenBank accession numbers AY790884 and AY799986-AY799998. The alignment for the genomic sequence of tgCA between positions 101 and 1810 of the cDNA has been submitted to EMBL-ALIGN database under the accession number ALIGN_000833. This report describes the presence of a unique dual domain carbonic anhydrase CA in the giant clam Tridacna gigas. CA plays an important role in the movement of inorganic carbon Ci from the surrounding seawater to the symbiotic algae that are found within the clam s tissue. One of these isoforms is a glycoprotein which is significantly larger 70 kDa than any previously reported from animals generally between 28 and 52 kDa . This a-family CA contains two complete carbonic anhydrase domains within the one protein accounting for its large size dual domain CAs have previously only been reported from two algal species. The protein contains a leader sequence an N-terminal CA domain and a C-terminal CA domain. The two CA domains have relatively little identity at the amino acid level 29 . The genomic sequence spans in excess of 17 kb and contains at least 12 introns and 13 exons. A number of these introns are in positions that are only found in the membrane attached secreted CAs. This fact along with phylogenetic analysis suggests that this protein represents the second example of

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