Stanley, Desirée N and Raines, Christine A and Kerfeld, Cheryl A (2013) Comparative Analysis of 126 Cyanobacterial Genomes Reveals Evidence of Functional Diversity Among Homologs of the Redox-Regulated CP12 Protein. Plant Physiology, 161 (2). pp. 824-835. DOI https://doi.org/10.1104/pp.112.210542
Stanley, Desirée N and Raines, Christine A and Kerfeld, Cheryl A (2013) Comparative Analysis of 126 Cyanobacterial Genomes Reveals Evidence of Functional Diversity Among Homologs of the Redox-Regulated CP12 Protein. Plant Physiology, 161 (2). pp. 824-835. DOI https://doi.org/10.1104/pp.112.210542
Stanley, Desirée N and Raines, Christine A and Kerfeld, Cheryl A (2013) Comparative Analysis of 126 Cyanobacterial Genomes Reveals Evidence of Functional Diversity Among Homologs of the Redox-Regulated CP12 Protein. Plant Physiology, 161 (2). pp. 824-835. DOI https://doi.org/10.1104/pp.112.210542
Abstract
<jats:title>Abstract</jats:title> <jats:p>CP12 is found almost universally among photosynthetic organisms, where it plays a key role in regulation of the Calvin cycle by forming a ternary complex with glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase. Newly available genomic sequence data for the phylum Cyanobacteria reveals a heretofore unobserved diversity in cyanobacterial CP12 proteins. Cyanobacterial CP12 proteins can be classified into eight different types based on primary structure features. Among these are CP12-CBS (for cystathionine-β-synthase) domain fusions. CBS domains are regulatory modules for a wide range of cellular activities; many of these bind adenine nucleotides through a conserved motif that is also present in the CBS domains fused to CP12. In addition, a survey of expression data sets shows that the CP12 paralogs are differentially regulated. Furthermore, modeling of the cyanobacterial CP12 protein variants based on the recently available three-dimensional structure of the canonical cyanobacterial CP12 in complex with GAPDH suggests that some of the newly identified cyanobacterial CP12 types are unlikely to bind to GAPDH. Collectively these data show that, as is becoming increasingly apparent for plant CP12 proteins, the role of CP12 in cyanobacteria is likely more complex than previously appreciated, possibly involving other signals in addition to light. Moreover, our findings substantiate the proposal that this small protein may have multiple roles in photosynthetic organisms.</jats:p>
Item Type: | Article |
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Uncontrolled Keywords: | Cyanobacteria; Bacterial Proteins; Phylogeny; Species Specificity; Amino Acid Sequence; Protein Conformation; Oxidation-Reduction; Genome, Bacterial; Models, Molecular; Genetic Variation |
Subjects: | Q Science > QH Natural history > QH301 Biology |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 13 Mar 2013 20:53 |
Last Modified: | 30 Oct 2024 19:43 |
URI: | http://repository.essex.ac.uk/id/eprint/5838 |