Altering the N-terminal arms of the polymerase manager protein UmuD modulates protein interactions.

Murison, David A; Ollivierre, Jaylene N; Huang, Qiuying; Budil, David E; Beuning, Penny J

Murison, David A; Ollivierre, Jaylene N; Huang, Qiuying; Budil, David E; Beuning, Penny J.

Affiliation

Murison DA; Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States of America.
Ollivierre JN; Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States of America.
Huang Q; Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States of America.
Budil DE; Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States of America.
Beuning PJ; Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States of America.

PLoS One ; 12(3): e0173388, 2017.

Article in En | MEDLINE | ID: mdl-28273172

Subject(s)

DNA-Directed DNA Polymerase/metabolism; Escherichia coli Proteins/metabolism; Protein Interaction Domains and Motifs; Amino Acid Sequence; Binding Sites; DNA Polymerase III/chemistry; DNA Polymerase III/metabolism; DNA-Directed DNA Polymerase/chemistry; DNA-Directed DNA Polymerase/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Homologous Recombination; Models, Molecular; Mutagenesis/radiation effects; Protein Binding; Protein Conformation; Protein Interaction Domains and Motifs/genetics; Protein Subunits/chemistry; Protein Subunits/metabolism; Sequence Deletion; Substrate Specificity; Ultraviolet Rays/adverse effects

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Full text: 1 Database: MEDLINE Main subject: Escherichia coli Proteins / DNA-Directed DNA Polymerase / Protein Interaction Domains and Motifs Type of study: Prognostic_studies Language: En Year: 2017 Type: Article

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