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High mobility group chromosomal protein 1 binds to the adeno‐associated virus replication protein (Rep) and promotes Rep‐mediated site‐specific cleavage of DNA, ATPase activity and transcriptional repression
Author(s) -
Costello Eithne,
Saudan Philippe,
Winocour Ernest,
Pizer Lewis,
Beard Peter
Publication year - 1997
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/16.19.5943
Subject(s) - biology , ter protein , high mobility group , dna replication , seqa protein domain , cleavage (geology) , origin recognition complex , psychological repression , dna , microbiology and biotechnology , replication factor c , replication protein a , dna binding protein , genetics , origin of replication , control of chromosome duplication , gene , eukaryotic dna replication , transcription factor , gene expression , fracture (geology) , paleontology
High mobility group protein 1 (HMG1) is an abundant non‐histone chromosomal protein which plays a role in several nuclear events involving DNA. Here we demonstrate that HMG1 physically interacts with the human adeno‐associated virus (AAV) Rep protein. HMG1 promotes the formation of Rep–DNA complexes and stimulates the activity of Rep in site‐ and strand‐specific cleavage of DNA and the hydrolysis of ATP, functions required for viral gene regulation, replication and site‐specific integration of viral DNA into human chromosome 19. We show that HMG1 enhances Rep‐mediated repression of the AAV p5 promoter in transfected cells, suggesting that HMG1 and Rep also interact in vivo . HMG1, Rep and DNA can be immunoprecipitated as a ternary complex. Kinetic studies indicate that complexes of Rep with DNA have similar stabilities in the presence and absence of HMG1.These results suggest that the effect of HMG1 on Rep binding is exerted at the step of complex formation and thereby may reflect an activity of HMG1 in promoting the assembly of complex cellular nucleoprotein structures.