Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition.

Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition. Research Abstract Details 

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Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition. Abstract Text:

Janice M Yoshizawa,Changzheng Li,Paul D Gershon,

Vaccinia poly(A) polymerase (VP55) interacts with > or = 33-nucleotide (nt) primers via uridylates at two sites (-27/-26 and -10). It adds approximately 30-nt poly(A) tails with a rapid, processive burst in which the first few nt are added without substantial primer movement, and addition of the remaining adenylates is dependent upon a six-uridylate tract at the extreme 3' end of the primer and accompanied by polymerase translocation. Interaction of VP55 with 2-aminopurine (2-AP)-containing primers was associated with a 3-fold enhancement in 2-AP fluorescence. In stopped-flow experiments, fluorescence intensity changed with time during the polyadenylation burst in a manner dependent upon the position of 2-AP, indicating a non-uniform isomerization of the polymerase-primer complex with time consistent with a discontinuous (saltatory) translocation mechanism. Three distinct translocatory phases could be discerned: a -10(U)-binding site forward movement, a -27/-26(UU)-binding site jump to -10, then a -27/-26(UU)-binding site movement further downstream. Poly(A) tail elongation showed no apparent pauses during these isomerizations. Fluorescence changes during polyadenylation of 2-AP-containing primers with short preformed oligo(A) tails reinforced the above observations. Primers composed entirely of oligo(U) (apart from the 2-AP sensor), in which the polymerase modules might be most able to "slide" uniformly, also showed the characteristic saltatory pattern of translocation. These data indicate, for the first time, a discontinuous mode of translocation for a non-templated polymerase.

Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition. Publishing Authors By Initials

JM Yoshizawa,C Li,PD Gershon,

For similar viruses: dna viruses: poxviridae: chordopoxvirinae: orthopoxvirus: vaccinia virus research abstracts see: viruses: dna viruses: poxviridae: chordopoxvirinae: orthopoxvirus: vaccinia virus research

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Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 19144-51

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 8

MONTH: 05

YEAR: 2007

Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition. Keywords Mesh Terms:

KEYWORDS: Vaccinia virus

MESH TERMS: genetics

Chemical & Substance for Abstract: Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition. Information

Substance Name: Polynucleotide Adenylyltransferase

Registry Number: EC 2.7.7.19

Grant and Affiliation Information for Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition.

AFFILIATION: Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697, USA.

Country: United States

AGENCY: United States NIAID

GRANT: T32AI007319-19

ACRONYM: AI

MEDLINETA: J Biol Chem

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