Rev1 Employs a Novel Mechanism of DNA Synthesis using a Protein Template

Journal Article · Sat Jan 01 04:00:00 EST 2005 · Science

DOI:https://doi.org/10.1126/science.1116336· OSTI ID:913716

Nair, D; Johnson, R; Prakash, L; Prakash, S; Aggarwal, A

The Rev1 DNA polymerase is highly specialized for the incorporation of C opposite template G. We present here the crystal structure of yeast Rev1 bound to template G and incoming 2'-deoxycytidine 5'-triphosphate (dCTP), which reveals that the polymerase itself dictates the identity of the incoming nucleotide, as well as the identity of the templating base. Template G and incoming dCTP do not pair with each other. Instead, the template G is evicted from the DNA helix, and it makes optimal hydrogen bonds with a segment of Rev1. Also, unlike other DNA polymerases, incoming dCTP pairs with an arginine rather than the templating base, which ensures the incorporation of dCTP over other incoming nucleotides. This mechanism provides an elegant means for promoting proficient and error-free synthesis through N2-adducted guanines that obstruct replication.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 913716
• Report Number(s): BNL--78284-2007-JA
• Journal Information: Science, Journal Name: Science Vol. 309; ISSN 0193-4511; ISSN SCEHDK
• Country of Publication: United States
• Language: English

Related Subjects

08 HYDROGEN
36 MATERIALS SCIENCE
ARGININE
CRYSTAL STRUCTURE
DNA
DNA POLYMERASES
HYDROGEN
NUCLEOTIDES
POLYMERASES
PROTEINS
SYNTHESIS
YEASTS
national synchrotron light source