| Literature DB >> 9473666 |
A Yamamoto1, A Iwata, Y Koh, S Kawai, S Murayama, K Hamada, S Maekawa, S Ueda, Y Sokawa.
Abstract
We have isolated two types of chicken 2',5'-oligoadenylate synthetase cDNAs, A and B, which encode predicted proteins of 508 amino acids (58316 Da) and 476 amino acids (54336 Da), respectively. The region of A-protein comprising 33 amino acid residues from 385Ala to 417Cys is substituted by a single amino acid 385Tyr in B-protein. The homology between chicken and mammalian 2',5'-oligoadenylate synthetases is 49.5% over the amino-terminal 337 residues. Proteins expressed from A- and B-cDNAs in E. coli cells were both active in synthesizing 2',5'-oligoadenylate. However, the activity of B-protein was 10-15% of that of A-protein. Southern blotting hybridization indicated that the chicken synthetases are encoded by a single gene. RT-PCR and PCR analyses of RNA and DNA of chicken erythrocytes together with the sequence data of the PCR products showed that A- and B-mRNAs are derived from alleles at a single locus encoding chicken 2',5'-oligoadenylate synthetase, designated as OAS * A and OAS * B. Chickens carrying OAS * A/B produce two types of synthetase with molecular masses of 58 and 54 kDa, and those carrying OAS * A/A produce only a single type of 58 kDa.Entities:
Mesh:
Substances:
Year: 1998 PMID: 9473666 DOI: 10.1016/s0167-4781(97)00148-6
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002