Association and dissociation of the GlnK-AmtB complex in response to cellular nitrogen status can occur in the absence of GlnK post-translational modification

Frontiers in Microbiology

Volumn 5, Issue DEC, 2014, Pages

  Radchenko, Martha V ^a,b   Thornton, Jeremy ^a   Merrick, Mike ^a  

^a JOHN INNES CENTRE   (United Kingdom)

^b ROSALIND FRANKLIN UNIVERSITY OF MEDICINE AND SCIENCE   (United States)

Author keywords

Ammonium transport; Amtb; Glnk; PII protein; Post translational modification; Uridylylation

Indexed keywords

2 OXOGLUTARIC ACID; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; MEMBRANE PROTEIN; NITROGEN; NITROGEN REGULATORY PROTEIN; PROTEIN AMTB; PROTEIN GLNK; PROTEIN VARIANT; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; COMPLEX FORMATION; CONTROLLED STUDY; ESCHERICHIA COLI; GENE OVEREXPRESSION; GENETIC ASSOCIATION; NITROGEN METABOLISM; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN EXPRESSION; PROTEIN INTERACTION ASSAY; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; WESTERN BLOTTING;

ESCHERICHIA COLI;

EID: 84920693304     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00731     Document Type: Article

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