JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ong, L. J.
Right arrow Articles by Glazer, A. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ong, L. J.
Right arrow Articles by Glazer, A. N.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 266, Issue 15, 9515-9527, 05, 1991

Phycoerythrins of marine unicellular cyanobacteria. I. Bilin types and locations and energy transfer pathways in Synechococcus spp. phycoerythrins

LJ Ong and AN Glazer
Division of Biochemistry and Molecular Biology, University of California, Berkeley 94720.

Marine Synechococcus strains WH8103, WH8020, and WH7803 each possess two different phycoerythrins, PE(II) and PE(I), in a weight ratio of 2- 4:1. PE(II) and PE(I) differ in amino acid sequence and in bilin composition and content. Studies with strain WH7803 indicated that both PE(II) and PE(I) were present in the same phycobilisome rod substructures and that energy absorbed by PE(II) was transferred to PE(I). Strain WH8103 and WH8020 PE(I)s carried five bilin chromophores thioether-linked to cysteine residues in sequences homologous to those previously characterized in C-, B-, and R-PEs. In contrast, six bilins were attached to strain WH8103 and WH8020 PE(II)s. Five of these were at positions homologous to bilin attachment sites in other phycoerythrins. The additional bilin attachment site was on the alpha subunit. The locations and bilin types in these PE(s) and in the marine Synechocystis strain WH8501 PE(I) (Swanson, R. V., Ong, L. J., Wilbanks, S. M., and Glazer, A. N. (1991) J. Biol. Chem. 266, 9528- 9534) are: (table; see text) Since phycourobilin (PUB) (lambda max approximately 495 nm) transfers energy to phycoerythrobilin (PEB) (lambda max approximately 550 nm), inspection of these data shows that the invariant PEB group at beta-82 is the terminal energy acceptor in phycoerythrins. The adaptations to blue-green light, high PUB content and the presence of an additional bilin on the alpha subunit, increase the efficiency of light absorption by PE(II)s at approximately 500 nm.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
C. Everroad, C. Six, F. Partensky, J.-C. Thomas, J. Holtzendorff, and A. M. Wood
Biochemical Bases of Type IV Chromatic Adaptation in Marine Synechococcus spp.
J. Bacteriol., May 1, 2006; 188(9): 3345 - 3356.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
C. Six, J.-C. Thomas, L. Thion, Y. Lemoine, F. Zal, and F. Partensky
Two Novel Phycoerythrin-Associated Linker Proteins in the Marine Cyanobacterium Synechococcus sp. Strain WH8102
J. Bacteriol., March 1, 2005; 187(5): 1685 - 1694.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
G. Rocap, D. L. Distel, J. B. Waterbury, and S. W. Chisholm
Resolution of Prochlorococcus and Synechococcus Ecotypes by Using 16S-23S Ribosomal DNA Internal Transcribed Spacer Sequences
Appl. Envir. Microbiol., March 1, 2002; 68(3): 1180 - 1191.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
C. S. Ting, G. Rocap, J. King, and S. W. Chisholm
Phycobiliprotein genes of the marine photosynthetic prokaryote Prochlorococcus: evidence for rapid evolution of genetic heterogeneity
Microbiology, November 1, 2001; 147(11): 3171 - 3182.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
N. Frankenberg, K. Mukougawa, T. Kohchi, and J. C. Lagarias
Functional Genomic Analysis of the HY2 Family of Ferredoxin-Dependent Bilin Reductases from Oxygenic Photosynthetic Organisms
PLANT CELL, April 1, 2001; 13(4): 965 - 978.
[Abstract] [Full Text]

Home page
 Appl. Environ. Microbiol.Home page
B. Palenik
Chromatic Adaptation in Marine Synechococcus Strains
Appl. Envir. Microbiol., February 1, 2001; 67(2): 991 - 994.
[Abstract] [Full Text]

Home page
 Appl. Environ. Microbiol.Home page
G. Toledo, B. Palenik, and B. Brahamsha
Swimming Marine Synechococcus Strains with Widely Different Photosynthetic Pigment Ratios Form a Monophyletic Group
Appl. Envir. Microbiol., December 1, 1999; 65(12): 5247 - 5251.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
J.-C. Thomas and C. Passaquet
Characterization of a Phycoerythrin without alpha -Subunits from a Unicellular Red Alga
J. Biol. Chem., January 22, 1999; 274(4): 2472 - 2482.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. MacColl, L. E. Eisele, E. C. Williams, and S. S. Bowser
The Discovery of a Novel R-phycoerythrin from an Antarctic Red Alga
J. Biol. Chem., July 19, 1996; 271(29): 17157 - 17160.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. J. J. C. F. Chan, and Alexander N. Glazer and L. J. Jung
Candidate Genes for the Phycoerythrocyanin [IMAGE] Subunit Lyase
J. Biol. Chem., May 26, 1995; 270(21): 12877 - 12884.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1991 by the American Society for Biochemistry and Molecular Biology.