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Journal of Bacteriology, August 2009, p. 4863-4869, Vol. 191, No. 15
0021-9193/09/$08.00+0     doi:10.1128/JB.00557-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Mutations at pipX Suppress Lethality of PII-Deficient Mutants of Synechococcus elongatus PCC 7942{triangledown}

Javier Espinosa, Miguel Angel Castells, Karim Boumediene Laichoubi, and Asunción Contreras*

División de Genética, Universidad de Alicante, Apartado 99, E-03080 Alicante, Spain

Received 27 April 2009/ Accepted 26 May 2009

The PII proteins are found in all three domains of life as key integrators of signals reflecting the balance of nitrogen and carbon. Genetic inactivation of PII proteins is typically associated with severe growth defects or death. However, the molecular basis of these defects depends on the specific functions of the proteins with which PII proteins interact to regulate nitrogen metabolism in different organisms. In Synechococcus elongatus PCC 7942, where PII forms complexes with the NtcA coactivator PipX, attempts to engineer PII-deficient strains failed in a wild-type background but were successful in pipX null mutants. Consistent with the idea that PII is essential to counteract the activity of PipX, four different spontaneous mutations in the pipX gene were found in cultures in which glnB had been genetically inactivated.


* Corresponding author. Mailing address: División de Genética, Facultad de Ciencias, Universidad de Alicante, E-03080 Alicante, Spain. Phone: 34 96 590 3957. Fax: 34 96 590 9569. E-mail: contrera{at}ua.es

{triangledown} Published ahead of print on 29 May 2009.


Journal of Bacteriology, August 2009, p. 4863-4869, Vol. 191, No. 15
0021-9193/09/$08.00+0     doi:10.1128/JB.00557-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.