Widespread but Small-Scale Changes in the Structural and Dynamic Properties of Vaccinia Virus Poly(A) Polymerase upon Association with Its Processivity Factor in Solution
Author:
Affiliation:
1. Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi100166x
Reference63 articles.
1. Poly(A) polymerase and a dissociable polyadenylation stimulatory factor encoded by vaccinia virus
2. Transition from rapid processive to slow nonprocessive polyadenylation by vaccinia virus poly(A) polymerase catalytic subunit is regulated by the net length of the poly(A) tail.
3. Molecular Flexibility and Discontinuous Translocation of a Non-templated Polymerase
4. Saltatory Forward Movement of a Poly(A) Polymerase during Poly(A) Tail Addition
5. Structural Basis for Sequence-Nonspecific Recognition of 5′-Capped mRNA by a Cap-Modifying Enzyme
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