The Role of Specialized Nucleoprotein Structures in Site-specific Recombination and Initiation of DNA Replication

1984 ◽  
Vol 49 (0) ◽  
pp. 727-733 ◽  
Author(s):  
H. Echols ◽  
M. Dodson ◽  
M. Better ◽  
J.D. Roberts ◽  
R. McMacken
1993 ◽  
Vol 58 (0) ◽  
pp. 475-485 ◽  
Author(s):  
D.M. Gilbert ◽  
H. Miyazawa ◽  
F.S. Nallaseth ◽  
J.M. Ortega ◽  
J.J. Blow ◽  
...  

2005 ◽  
Vol 79 (13) ◽  
pp. 8661-8664 ◽  
Author(s):  
Stephen Schuck ◽  
Arne Stenlund

ABSTRACT Viral initiator proteins are polypeptides that form oligomeric complexes on the origin of DNA replication (ori). These complexes carry out a multitude of functions related to initiation of DNA replication, and although many of these functions have been characterized biochemically, little is understood about how the complexes are assembled. Here we demonstrate that loss of one particular interaction, the dimerization between E1 DNA binding domains, has a severe effect on DNA replication in vivo but has surprisingly modest effects on most individual biochemical activities in vitro. We conclude that the dimer interaction is primarily required for initial recognition of ori.


2004 ◽  
Vol 48 (3) ◽  
pp. 1028-1031 ◽  
Author(s):  
Sally A. Turner ◽  
Shelley N. Luck ◽  
Harry Sakellaris ◽  
Kumar Rajakumar ◽  
Ben Adler

ABSTRACT The Shigella resistance locus (SRL) pathogenicity island (PAI) in Shigella spp. mediates resistance to streptomycin, ampicillin, chloramphenicol, and tetracycline. It can be excised from the chromosome via site-specific recombination mediated by the P4-related int gene. Here, we show that SRL PAI attP is capable of RecA-independent, site-specific, int-mediated integration into two bacterial tRNA attB sites.


1980 ◽  
Vol 138 (3) ◽  
pp. 503-512 ◽  
Author(s):  
Susan Gottesman ◽  
Ken Abremski

1979 ◽  
Vol 43 (0) ◽  
pp. 1121-1126 ◽  
Author(s):  
H. I. Miller ◽  
A. Kikuchi ◽  
H. A. Nash ◽  
R. A. Weisberg ◽  
D. I. Friedman

1993 ◽  
Vol 58 (0) ◽  
pp. 505-513 ◽  
Author(s):  
P. Merker ◽  
G. Muskhelishvili ◽  
A. Deufel ◽  
K. Rusch ◽  
R. Kahmann

Blood ◽  
2001 ◽  
Vol 97 (5) ◽  
pp. 1266-1273 ◽  
Author(s):  
Sumiko Watanabe ◽  
Rong Zeng ◽  
Yutaka Aoki ◽  
Tohru Itoh ◽  
Ken-ichi Arai

Several lines of evidence indicate that transcriptional activation is coupled with DNA replication initiation, but the nature of initiation of DNA replication in mammalian cells is unclear. Polyoma virus replicon is an excellent system to analyze the initiation of DNA replication in murine cells because its replication requires an enhancer, and all components of replication machinery, except for DNA helicase large T antigen, are supplied by host cells. This system was used to examine the role of signal transducer and activator of transcription (STAT5) in replication initiation of polyoma replicon in the mouse lymphoid cell line BA/F3. The plasmid with tandem repeats of consensus STAT5 binding sites followed by polyoma replication origin was replicated by stimulation with human granulocyte-macrophage colony-stimulating factor (hGM-CSF) in the presence of polyoma large T antigen in BA/F3 cells. Mutation analysis of the hGM-CSF receptor β subunit revealed that only the box1 region is essential, and the C-terminal tyrosine residues are dispensable for the activity. Addition of the tyrosine kinase inhibitor genistein suppressed this replication without affecting transcriptional activation of STAT5. Because deletion analysis of STAT5 indicates the importance of the C-terminal transcriptional activation domain of STAT5 for the initiation of replication, the role of this region in the activation of replication was examined with a GAL4–STAT5 fusion protein. GAL4–STAT5 activated replication of the plasmid containing tandem repeats of GAL4 binding sites and polyoma replication origin in BA/F3 cells. Mutation analysis of GAL4–STAT5 indicated that multiple serine residues coordinately have a role in activating replication. This is the first direct evidence indicating the potential involvement of STAT5 in replication.


2021 ◽  
Author(s):  
Ilaria Volpi ◽  
Peter J. Gillespie ◽  
Gaganmeet Singh Chadha ◽  
J. Julian Blow

AbstractTreslin/Ticrr is required for the initiation of DNA replication and binds to MTBP (Mdm2 Binding Protein). Here we show that in Xenopus egg extract, MTBP forms an elongated tetramer with Treslin containing two molecules of each protein. Immunodepletion and add-back experiments show that Treslin-MTBP is rate-limiting for replication initiation. It is recruited onto chromatin before S phase starts and recruitment continues during S phase. We show that DDK activity both increases and strengthens the interaction of Treslin-MTBP with licensed chromatin. We also show that DDK activity cooperates with CDK activity to drive the interaction of Treslin-MTBP with TopBP1 which is a regulated crucial step in pre-Initiation Complex formation. These results suggest how DDK works together with CDKs to regulate Treslin-MTBP and plays a crucial in selecting which origins will undergo initiation.


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