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PMID: 1391782 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Sequence comparison of two highly homologous phycoerythrins differing in bilin composition.

Plant molecular biology ·Vol. 20 ·No. 2 ·1992-10-00 ·Pages 353-6

de Lorimier R, Chen CC, Glazer AN

Abstract

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.

MeSH Terms
Amino Acid Sequence Bile Pigments/analysis Cyanobacteria/genetics Molecular Sequence Data Phycoerythrin/chemistry,genetics Sequence Homology
Chemicals
Bile Pigments Phycoerythrin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
de Lorimier R
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Chen C C
Glazer A N
References (8)
8 references, click to expand
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Article Info
Journal
Plant molecular biology
Abbr.
Plant Mol Biol
ISSN
0167-4412
DOI
10.1007/BF00014507
Published
1992-10-00
Pages
353-6
Language
English
Region
Netherlands
NLM ID
9106343
Subset
IM
Grants
NIGMS NIH HHS · GM 28994 · United States
Databases
GENBANK
M91809
External Links
PubMed source DOI: 10.1007/BF00014507 View journal details
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