scholarly journals The ammonium-inactivated cyanobacterial glutamine synthetase I is reactivatedin vivoby a mechanism involving proteolytic removal of its inactivating factors

2007 ◽  
Vol 65 (1) ◽  
pp. 166-179 ◽  
Author(s):  
Carla V. Galmozzi ◽  
M. Jesús Fernández-Avila ◽  
José C. Reyes ◽  
Francisco J. Florencio ◽  
M. Isabel Muro-Pastor
1988 ◽  
Vol 26 (9-10) ◽  
pp. 571-584 ◽  
Author(s):  
Corrado Caggese ◽  
Ruggiero Caizzi ◽  
Maria Pia Bozzetti ◽  
Paolo Barsanti ◽  
Ferruccio Ritossa

1992 ◽  
Vol 13 (5) ◽  
pp. 359-366 ◽  
Author(s):  
Corrado Caggese ◽  
Ruggiero Caizzi ◽  
Paolo Barsanti ◽  
Maria Pia Bozzetti

1981 ◽  
Vol 5 (6) ◽  
pp. 329-331 ◽  
Author(s):  
Chandra Shekhar Nautiyal ◽  
Vinod V. Modi

2014 ◽  
Vol 171 (5) ◽  
pp. 104-108 ◽  
Author(s):  
Sirinapa Chungopast ◽  
Pilunthana Thapanapongworakul ◽  
Hiroyuki Matsuura ◽  
Tan Van Dao ◽  
Toshimasa Asahi ◽  
...  

2001 ◽  
Vol 14 (7) ◽  
pp. 823-831 ◽  
Author(s):  
Rosarita Tatè ◽  
Luigi Mandrich ◽  
Maria R. Spinosa ◽  
Anna Riccio ◽  
Alessandro Lamberti ◽  
...  

We show that the protein encoded by the glutamine synthetase translational inhibitor (gstI) gene reduces the NH4+ assimilation capacity of Rhizobium leguminosarum. In this organism, gstI expression is regulated by the ntr system, including the PII protein, as a function of the nitrogen (N) status of the cells. The GstI protein, when expressed from an inducible promoter, inhibits glutamine synthetase II (glnII) expression under all N conditions tested. The induction of gstI affects the growth of a glutamine synthetase I (glnA-) strain and a single amino acid substitution (W48D) results in the complete loss of GstI function. During symbiosis, gstI is expressed in young differentiating symbiosomes (SBs) but not in differentiated N2-fixing SBs. In young SBs, the PII protein modulates the transcription of NtrC-regulated genes such as gstI and glnII. The evidence presented herein strengthens the idea that the endocytosis of bacteria inside the cytoplasm of the host cells is a key step in the regulation of NH4+ metabolism.


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