Location of Repository

The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 is modified by serine phosphorylation and signals the cellular N-status.

By K Forchhammer and N Tandeau de Marsac

Abstract

The glnB gene product (PII protein) from Synechococcus sp. has previously been identified among 32P-labeled proteins, and its modification state has been observed to depend on both the nitrogen source and the spectral light quality (N. F. Tsinoremas, A. M. Castets, M. A. Harrison, J. F. Allen, and N. Tandeau de Marsac, Proc. Natl. Acad. Sci. USA 88:4565-4569, 1991). As shown in this study, modification of the PII protein primarily responds to the N-status of the cell, and its light-dependent variations are are mediated through nitrate metabolism. Modification of the PII protein results in the appearance of three isomeric forms with increasing negative charge. Unlike its homolog counterparts characterized so far, PII in Synechococcus sp. is modified by phosphorylation on a serine residue, which represents a unique kind of protein modification in bacterial nitrogen signalling pathways

Topics: Research Article
Year: 1994
OAI identifier: oai:pubmedcentral.nih.gov:205017
Provided by: PubMed Central
Sorry, our data provider has not provided any external links therefor we are unable to provide a PDF.

Suggested articles


To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.