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Gene Review:

prk - phosphoribulokinase

Synechocystis sp. PCC 6803

This record was discontinued.

Su, X. et al., van Thor, J.J. et al., Wedel, N. et al.

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Disease relevance of prk

A residue substitution in phosphoribulokinase of Synechocystis PCC 6803 renders the mutant light-sensitive [1].

High impact information on prk

Evolutionary conserved light regulation of Calvin cycle activity by NADPH-mediated reversible phosphoribulokinase/CP12/ glyceraldehyde-3-phosphate dehydrogenase complex dissociation [2].
An open reading frame is found to encode phosphoribulokinase, a key enzyme in the enzyme system for photosynthetic carbon reduction (ES-PCR) [1].
The mutation responsible for the phenotype of BRLS is a single nucleotide change that results in substitution of phenylalanine for Ser-222 in the phosphoribulokinase [1].
A model for a new type of bidirectional operator, regulating the expression of petH and prk, is proposed [3].
The transcription start site of the prk transcript was mapped 219 bp upstream of the initiation codon, resulting in a 223 bp antisense region between both transcripts [3].

References

A residue substitution in phosphoribulokinase of Synechocystis PCC 6803 renders the mutant light-sensitive. Su, X., Bogorad, L. J. Biol. Chem. (1991) [Pubmed]
Evolutionary conserved light regulation of Calvin cycle activity by NADPH-mediated reversible phosphoribulokinase/CP12/ glyceraldehyde-3-phosphate dehydrogenase complex dissociation. Wedel, N., Soll, J. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
Characterization and transcriptional regulation of the Synechocystis PCC 6803 petH gene, encoding ferredoxin-NADP+ oxidoreductase: involvement of a novel type of divergent operator. van Thor, J.J., Hellingwerf, K.J., Matthijs, H.C. Plant Mol. Biol. (1998) [Pubmed]

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