The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide

FEBS Letters

Volumn 589, Issue 2, 2015, Pages 201-206

  Conti, Joseph ^a   Viola, Marissa G ^a   Camberg, Jodi L ^a  

^a UNIVERSITY OF RHODE ISLAND   (United States)

Author keywords

ATPase; Cytokinesis; Min system; MinE; Phospholipids

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; MINC PROTEIN; MIND PROTEIN; MINE PROTEIN; MUTANT PROTEIN; NUCLEOTIDE; PHOSPHOLIPID; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; ESCHERICHIA COLI PROTEIN; MEMBRANE PROTEIN; MINC PROTEIN, E COLI; MIND PROTEIN, E COLI;

ARTICLE; BACTERIAL METABOLISM; CELL DIVISION; COMPLEX FORMATION; CONTROLLED STUDY; GENE MUTATION; MOLECULAR STABILITY; NONHUMAN; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN POLYMERIZATION; PROTEIN PROTEIN INTERACTION; ULTRACENTRIFUGATION; CHEMICAL STRUCTURE; CHEMISTRY; CYTOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; MICROBIAL VIABILITY; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; ULTRASTRUCTURE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; MICROBIAL VIABILITY; MICROSCOPY, ELECTRON, TRANSMISSION; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY;

EID: 84920744608     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.11.047     Document Type: Article

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