Fremyella diplosiphon

2019 ◽  
Vol 27 (6) ◽  
pp. 562-563
Author(s):  
Allissa M. Haney ◽  
David M. Kehoe
Keyword(s):  
Fremyella Diplosiphon

CpeR is an activator required for expression of the phycoerythrin operon (cpeBA) in the cyanobacterium Fremyella diplosiphon and is encoded in the phycoerythrin linker-polypeptide operon (cpeCDESTR)

2002 ◽  
Vol 44 (6) ◽  
pp. 1517-1531 ◽  
Author(s):  
John G. Cobley ◽  
A. Clay Clark ◽  
Siromi Weerasurya ◽  
F. Anne Queseda ◽  
Jimmy Y. Xiao ◽  
...  
Keyword(s):  
Fremyella Diplosiphon

scholarly journals Light Quantity Affects the Regulation of Cell Shape in Fremyella diplosiphon

2012 ◽  
Vol 3 ◽  
Author(s):  
Bagmi Pattanaik ◽  
Melissa J. Whitaker ◽  
Beronda L. Montgomery
Keyword(s):  
Cell Shape ◽  
Fremyella Diplosiphon ◽  
Light Quantity

Identification of a Halotolerant Mutant via In Vitro Mutagenesis in the Cyanobacterium Fremyella diplosiphon

2016 ◽  
Vol 74 (1) ◽  
pp. 77-83 ◽  
Author(s):  
Behnam Tabatabai ◽  
AnithaChristy S. Arumanayagam ◽  
Oluwatomisin Enitan ◽  
Arunmani Mani ◽  
Savithiry S. Natarajan ◽  
...  
Keyword(s):  
In Vitro Mutagenesis ◽  
Fremyella Diplosiphon

scholarly journals AplA, a Member of a New Class of Phycobiliproteins Lacking a Traditional Role in Photosynthetic Light Harvesting

2004 ◽  
Vol 186 (21) ◽  
pp. 7420-7428 ◽  
Author(s):  
Beronda L. Montgomery ◽  
Elena Silva Casey ◽  
Arthur R. Grossman ◽  
David M. Kehoe
Keyword(s):  
Amino Acid ◽  
Tertiary Structure ◽  
Light Harvesting ◽  
Water Soluble ◽  
Amino Acid Residues ◽  
Subunit Interactions ◽  
Traditional Role ◽  
Light Harvesting Complexes ◽  
Fremyella Diplosiphon ◽  
New Class

ABSTRACT All known phycobiliproteins have light-harvesting roles during photosynthesis and are found in water-soluble phycobilisomes, the light-harvesting complexes of cyanobacteria, cyanelles, and red algae. Phycobiliproteins are chromophore-bearing proteins that exist as heterodimers of α and β subunits, possess a number of highly conserved amino acid residues important for dimerization and chromophore binding, and are invariably 160 to 180 amino acids long. A new and unusual group of proteins that is most closely related to the allophycocyanin members of the phycobiliprotein superfamily has been identified. Each of these proteins, which have been named allophycocyanin-like (Apl) proteins, apparently contains a 28-amino-acid extension at its amino terminus relative to allophycocyanins. Apl family members possess the residues critical for chromophore interactions, but substitutions are present at positions implicated in maintaining the proper α-β subunit interactions and tertiary structure of phycobiliproteins, suggesting that Apl proteins are able to bind chromophores but fail to adopt typical allophycocyanin conformations. AplA isolated from the cyanobacterium Fremyella diplosiphon contained a covalently attached chromophore and, although present in the cell under a number of conditions, was not detected in phycobilisomes. Thus, Apl proteins are a new class of photoreceptors with a different cellular location and structure than any previously described members of the phycobiliprotein superfamily.

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