Heterotrimerization of PII-like signalling proteins: implications for PII-mediated signal transduction systems.

Abstract:

:PII-like signalling molecules are trimeric proteins composed of 12-13 kDa polypeptides encoded by the glnB gene family. Heterologous expression of a cyanobacterial glnB gene in Escherichia coli leads to an inactivation of E. coli's own PII signalling system. In the present work, we show that this effect is caused by the formation of functionally inactive heterotrimers between the cyanobacterial glnB gene product and the E. coli PII paralogues GlnB and GlnK. This led to the discovery that GlnK and GlnB of E. coli also form heterotrimers with each other. The influence of the oligomerization partner on the function of the single subunit was studied using heterotrimerization with the Synechococcus PII protein. Uridylylation of GlnB and GlnK was less efficient but still possible within these heterotrimers. In contrast, the ability of GlnB-UMP to stimulate the adenylyl-removing activity of GlnE (glutamine synthetase adenylyltransferase/removase) was almost completely abolished, confirming that rapid deadenylylation of glutamine synthetase upon nitrogen stepdown requires functional homotrimeric GlnB protein. Remarkably, however, rapid adenylylation of glutamine synthetase upon exposing nitrogen-starved cells to ammonium was shown to occur in the absence of a functional GlnB/GlnK signalling system as efficiently as in its presence.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Forchhammer K,Hedler A,Strobel H,Weiss V

doi

10.1046/j.1365-2958.1999.01477.x

subject

Has Abstract

pub_date

1999-07-01 00:00:00

pages

338-49

issue

2

eissn

0950-382X

issn

1365-2958

pii

1477

journal_volume

33

pub_type

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