NDLI: Phosphorylation of the PII protein (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942: analysis of in vitro kinase activity.

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Phosphorylation of the PII protein (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942: analysis of in vitro kinase activity.

Content Provider	Semantic Scholar
Author	Forchhammer, Karl Marsac, Nicole Tandeau De
Copyright Year	1995
Abstract	The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 signals the cellular state of nitrogen assimilation relative to CO2 fixation by being phosphorylated at a seryl residue. In this study, we first determined the location of the phosphorylated seryl residue within the PII amino acid sequence. The phosphorylation site exhibits an RXS motif, a recognition sequence characteristic for cyclic AMP-dependent protein serine kinases from eukaryotes. We established an in vitro PII phosphorylation assay to further analyze the PII kinase activity in Synechococcus sp. strain PCC 7942. ATP was used specifically as a phosphoryl donor, and the PII kinase activity was shown to be stimulated by alpha-ketoglutarate. Unlike the PII-modifying uridylyltransferase- and uridylyl-removing enzyme characterized in proteobacteria, the activity of the PII kinase from the cyanobacterium did not respond to glutamine.
File Format	PDF HTM / HTML
DOI	10.1128/jb.177.20.5812-5817.1995
PubMed reference number	7592328
Journal	Medline
Volume Number	177
Issue Number	20
Alternate Webpage(s)	http://jb.asm.org/content/177/20/5812.full.pdf
Alternate Webpage(s)	https://doi.org/10.1128/jb.177.20.5812-5817.1995
Journal	Journal of bacteriology
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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