Characterization of the pet operon of Rhodospirillum rubrum

1992 ◽  
Vol 32 (2) ◽  
pp. 79-94 ◽  
Author(s):  
Savita Chankor ◽  
Carolyn Moomau ◽  
Saadettin G�ner ◽  
Joan Hsu ◽  
Mariko K. Tokito ◽  
...  
Keyword(s):  
Rhodospirillum Rubrum

CHARACTERIZATION OF ANTIMYCIN RESISTANT MUTANTS OF RHODOSPIRILLUM RUBRUM

1994 ◽  
Vol 22 (1) ◽  
pp. 59S-59S
Author(s):  
Joachim Uhrig ◽  
Christiane Jakobs ◽  
Christoph Majewski ◽  
Achim Trebst
Keyword(s):  
Rhodospirillum Rubrum ◽  
Resistant Mutants

Characterization of Rhodospirillum rubrum ST2. A new Tn5-induced carotenoid-less mutant for functional studies

1996 ◽  
Vol 151 (1) ◽  
pp. 57-61 ◽  
Author(s):  
Markus Wiggli ◽  
Luigi Cornacchia ◽  
Rudolf Saegesser ◽  
Reinhard Bachofen ◽  
Robin Ghosh
Keyword(s):  
Rhodospirillum Rubrum ◽  
Functional Studies

scholarly journals Mutagenesis and Functional Characterization of the Four Domains of GlnD, a Bifunctional Nitrogen Sensor Protein

2010 ◽  
Vol 192 (11) ◽  
pp. 2711-2721 ◽  
Author(s):  
Yaoping Zhang ◽  
Edward L. Pohlmann ◽  
Jose Serate ◽  
Mary C. Conrad ◽  
Gary P. Roberts
Keyword(s):  
Escherichia Coli ◽  
Functional Analysis ◽  
Nitrogen Assimilation ◽  
Rhodospirillum Rubrum ◽  
Functional Characterization ◽  
Enteric Bacteria ◽  
Truncated Protein ◽  
Primary Sensor ◽  
Sensor Protein

ABSTRACT GlnD is a bifunctional uridylyltransferase/uridylyl-removing enzyme (UTase/UR) and is believed to be the primary sensor of nitrogen status in the cell by sensing the level of glutamine in enteric bacteria. It plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of PII protein; PII in turn regulates a variety of other proteins. GlnD appears to have four distinct domains: an N-terminal nucleotidyltransferase (NT) domain; a central HD domain, named after conserved histidine and aspartate residues; and two C-terminal ACT domains, named after three of the allosterically regulated enzymes in which this domain is found. Here we report the functional analysis of these domains of GlnD from Escherichia coli and Rhodospirillum rubrum. We confirm the assignment of UTase activity to the NT domain and show that the UR activity is a property specifically of the HD domain: substitutions in this domain eliminated UR activity, and a truncated protein lacking the NT domain displayed UR activity. The deletion of C-terminal ACT domains had little effect on UR activity itself but eliminated the ability of glutamine to stimulate that activity, suggesting a role for glutamine sensing by these domains. The deletion of C-terminal ACT domains also dramatically decreased UTase activity under all conditions tested, but some of these effects are due to the competition of UTase activity with unregulated UR activity in these variants.

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