SEQUENCE COMPARISON OF 2 HIGHLY HOMOLOGOUS PHYCOERYTHRINS DIFFERING IN BILIN COMPOSITION

被引：8

作者：

DELORIMIER, R ^{[1
]}

CHEN, CCJ ^{[1
]}

GLAZER, AN ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY,DEPT MOLEC & CELL BIOL,DIV BIOCHEM & MOLEC BIOL,229 STANLEY HALL,BERKELEY,CA 94720

来源：

PLANT MOLECULAR BIOLOGY | 1992年 / 20卷 / 02期

关键词：

MARINE CYANOBACTERIA; PHYCOBILIPROTEIN; PHYCOERYTHROBILIN; PHYCOUROBILIN; SYNECHOCOCCUS SP STRAIN-WH8103;

D O I：

10.1007/BF00014507

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Genes encoding the alpha and beta-subunits of class II phycoerythrin from Synechococcus sp. strain WH8103 were cloned and sequenced. The deduced amino acid sequences were compared to class II phycoerythrin from Synechococcus sp. strain WH8020 and found to share 92% identity, yet the proteins differ in the bilin isomer (phycoerythrobilin versus phycourobilin) bound to two of the six chromophore attachment sites. Amino acid residues which might contact the bilin at each of the two variable sites were inferred by sequence alignment with phycocyanins. Putative bilin-contacting residues differing between the two phycoerythrins were identified which may determine bilin specificity.

引用

页码：353 / 356

页数：4

共 8 条

[1] ISOLATION, CRYSTALLIZATION, CRYSTAL-STRUCTURE ANALYSIS AND REFINEMENT OF CONSTITUTIVE C-PHYCOCYANIN FROM THE CHROMATICALLY ADAPTING CYANOBACTERIUM FREMYELLA-DIPLOSIPHON AT 1.66 A RESOLUTION [J].