The molecular weight distribution of succinoglycan produced by Sinorhizobium meliloti is influenced by specific tyrosine phosphorylation and ATPase activity of the cytoplasmic domain of the ExoP protein

Journal of Bacteriology

Volumn 183, Issue 17, 2001, Pages 5163-5170

  Niemeyer, D ^a   Becker, A ^a  

^a BIELEFELD UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID; DNA; PROTEIN; SUCCINOGLYCAN; TYROSINE;

ARTICLE; CYTOPLASM; DNA SEQUENCE; ENZYME ACTIVITY; GEL FILTRATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IMMUNOBLOTTING; MOLECULAR WEIGHT; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; PHOSPHORYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SINORHIZOBIUM MELILOTI; SITE DIRECTED MUTAGENESIS;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; BINDING SITES; CYTOPLASM; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENOTYPE; PHOSPHORYLATION; POLYSACCHARIDES, BACTERIAL; PROTEIN CONFORMATION; SINORHIZOBIUM MELILOTI; TYROSINE;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; SINORHIZOBIUM MELILOTI;

EID: 0034891240     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.183.17.5163-5170.2001     Document Type: Article

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