Schildgen, Oliver ORCID: 0000-0003-4297-9627 (2016). ATP binding leads to autophosphorylation of HSV-1 origin binding protein. Mol. Genet. Microbiol. Virol., 31 (3). S. 168 - 178. NEW YORK: ALLERTON PRESS INC. ISSN 1934-841X

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Abstract

The tsUL9 gene products exhibit a strongly reduced ATPase function at the nonpermissive temperature, an effect that can be compensated by the addition of unspecific DNA. Here it is demonstrated, that the reduced ATPase activity is caused by altered ATP binding of the tsOBP at the nonpermissive temperature. Furthermore the addition of unspecific DNA to the ATPase reaction not only compensates the ts phenotype at the nonpermissive temperature but also enhances the ATPase activity at the permissive temperature of both wild type and tsOBP. Thereby, the OBP becomes autophosphorylated. Moreover, addition of subgenomic HSV-1 DNA has no further enhancing effect, supporting the inchworm model for the HSV-OBP function.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Schildgen, OliverUNSPECIFIEDorcid.org/0000-0003-4297-9627UNSPECIFIED
URN: urn:nbn:de:hbz:38-270173
DOI: 10.3103/S0891416816030095
Journal or Publication Title: Mol. Genet. Microbiol. Virol.
Volume: 31
Number: 3
Page Range: S. 168 - 178
Date: 2016
Publisher: ALLERTON PRESS INC
Place of Publication: NEW YORK
ISSN: 1934-841X
Language: English
Faculty: Unspecified
Divisions: Unspecified
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
SIMPLEX-VIRUS TYPE-1; CONSERVED HELICASE MOTIFS; VIRAL-DNA REPLICATION; INCHWORM MECHANISM; UL9 PROTEIN; MUTANTS; TRANSDOMINANT; SUBSTRATE; REVEALS; ICP8Multiple languages
Biochemistry & Molecular Biology; MicrobiologyMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/27017

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