STRUCTURAL SIMILARITIES BETWEEN THE DEVELOPMENT-SPECIFIC PROTEIN-S FROM A GRAM-NEGATIVE BACTERIUM, MYXOCOCCUS-XANTHUS, AND CALMODULIN
STRUCTURAL SIMILARITIES BETWEEN THE DEVELOPMENT-SPECIFIC PROTEIN-S FROM A GRAM-NEGATIVE BACTERIUM, MYXOCOCCUS-XANTHUS, AND CALMODULIN
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DOI：
10.1073/pnas.80.22.6829
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发表时间：
1983-01-01
期刊：
影响因子：
--
通讯作者：
INOUYE, M
中科院分区：
文献类型：
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作者：
INOUYE, S;FRANCESCHINI, T;INOUYE, M
During differentiation of M. xanthus, a large amount of protein S is produced and assembled on the surface of the myxospore by a process that specifically requires Ca2+. The gene for protein S was cloned, and 2 tandemly repeated homologous genes were found within a short distance of each other in the M. xanthus chromosome. The DNA sequence of 3692 bp [base pairs] encompassing both genes was determined and the amino acid sequences of the 2 gene products were deduced. The gene 1 (upstream) product and the gene 2 (downstream) product show extensive amino acid sequence homology (88%). However, from their structures, protein S was produced from gene 2, indicating that gene 2 is specifically turned on during differentiation. The structure of protein S shows striking similarities with calmodulin: protein S is composed of 4 internally homologous domains. In particular, the first and the third domains, consisting of 38 residues each, show a high level of homology (79%), and the second and the fourth domains, consisting of 40 residues each, show homology of 65%. In the first and the third domains, there is a common sequence of 9 residues, Glu (or Asp)-Asn-Asn-Thr-Ile-Ser-Ser-Val-Lys, which is highly homologous to one of the proposed Ca2+-binding sequences in bovine brain calmodulin, Asp-Gly-Asn-Gly-Thr-Ile-Thr-Thr-Lys.
