Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile

Open Biology

Volumn 6, Issue 12, 2016, Pages

  Van Eijk, Erika ^a   Paschalis, Vasileios ^b   Green, Matthew ^b   Friggen, Annemieke H ^a   Larson, Marilynn A ^d,e   Spriggs, Keith ^c   Briggs, Geoffrey S ^b   Soultanas, Panos ^b   Smits, Wiep Klaas ^a  

^a LEIDEN UNIVERSITY MEDICAL CENTER   (Netherlands)

^b Center for Biomolecular Sciences   (Netherlands)

^c UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^d UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^e National Strategic Research Institute   (United States)

Author keywords

ATPase; Clostridium difficile; DNA replication initiation; Helicase loading and activation; Primase trinucleotide specificity

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL DNA; BACTERIAL PROTEIN; DNA HELICASE; DNA PRIMASE; PROTEIN BINDING;

CHEMISTRY; COMPUTER SIMULATION; DNA REPLICATION; ENZYMOLOGY; GENETICS; METABOLISM; MUTATION; PEPTOCLOSTRIDIUM DIFFICILE;

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; CLOSTRIDIUM DIFFICILE; COMPUTER SIMULATION; DNA HELICASES; DNA PRIMASE; DNA REPLICATION; DNA, BACTERIAL; MUTATION; PROTEIN BINDING;

EID: 85008153039     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.160272     Document Type: Article

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