Role of Tyr-22 in the Binding of Pf3 ssDNA Binding Protein to Nucleic Acids

Biochemistry ◽  
1995 ◽  
Vol 34 (16) ◽  
pp. 5635-5643 ◽  
Author(s):  
Michael D. Powell ◽  
Donald M. Gray
Keyword(s):  
Nucleic Acids ◽  
Binding Protein ◽  
Ssdna Binding ◽  
Ssdna Binding Protein

scholarly journals Compartmentalization of the replication fork by single-stranded DNA binding protein regulates translesion synthesis

2020 ◽  
Author(s):  
Seungwoo Chang ◽  
Elizabeth S. Thrall ◽  
Luisa Laureti ◽  
Vincent Pagès ◽  
Joseph J. Loparo
Keyword(s):  
Dna Replication ◽  
Binding Protein ◽  
Translesion Synthesis ◽  
Genome Maintenance ◽  
Ssdna Binding ◽  
Epsilon Subunit ◽  
Pol Iv ◽  
Ssdna Binding Protein ◽  
Pol Iii

AbstractDNA replication is mediated by the coordinated actions of multiple enzymes within replisomes. Processivity clamps tether many of these enzymes to DNA, allowing access to the primer/template junction. Many clamp-interacting proteins (CLIPs) are involved in genome maintenance pathways including translesion synthesis (TLS). Despite their abundance, DNA replication in bacteria is not perturbed by these CLIPs. Here we show that while the TLS polymerase Pol IV is largely excluded from moving replisomes, the remodeling of ssDNA binding protein (SSB) upon replisome stalling enriches Pol IV at replication forks. This enrichment is indispensable for Pol IV-mediated TLS on both the leading and lagging strands as it enables Pol IV-processivity clamp binding by overcoming the gatekeeping role of the Pol III epsilon subunit. As we have demonstrated for the Pol IV-SSB interaction, we propose that the binding of CLIPs to the processivity clamp must be preceded by interactions with factors that serve as localization markers for their site of action.

scholarly journals Cloning and characterisation of a nuclear, site specific ssDNA binding protein

1995 ◽  
Vol 23 (13) ◽  
pp. 2389-2395 ◽  
Author(s):  
Marten P. Smidt ◽  
Bernadetta Russchen ◽  
Lenie Snippe ◽  
Jan Wilnholds ◽  
Geert AB
Keyword(s):  
Binding Protein ◽  
Site Specific ◽  
Ssdna Binding ◽  
Nuclear Site ◽  
Ssdna Binding Protein

scholarly journals S. cerevisiae Srs2 helicase ensures normal recombination intermediate metabolism during meiosis and prevents accumulation of Rad51 aggregates

2019 ◽  
Author(s):  
Laura J Hunt ◽  
Emad Ahmed ◽  
Hardeep Kaur ◽  
Jasvinder Ahuja ◽  
Lydia Hulme ◽  
...  
Keyword(s):  
Mitotic Cell ◽  
Dna Helicase ◽  
Ssdna Binding ◽  
Meiotic Progression ◽  
Intermediate Metabolism ◽  
Ssdna Binding Protein ◽  
Srs2 Helicase ◽  
Strand Invasion ◽  
Functional Dna

We investigated the meiotic role of Srs2, a multi-functional DNA helicase/translocase that destabilizes Rad51-DNA filaments, and is thought to regulate strand invasion and prevent hyper-recombination during the mitotic cell cycle. We find that Srs2 activity is required for normal meiotic progression and spore viability. A significant fraction of srs2 mutant cells progress through both meiotic divisions without separating the bulk of their chromatin, although sister centromeres often separate. Undivided nuclei contain aggregates of Rad51 colocalized with the ssDNA-binding protein RPA, suggesting the presence of persistent single-strand DNA. Rad51 aggregate formation requires Spo11-induced DSBs, Rad51 strand-invasion activity, and progression past the pachytene stage of meiosis, but not the DSB end-resection or the bias towards inter-homologue strand invasion characteristic of normal meiosis. srs2 mutants also display altered meiotic recombination intermediate metabolism, revealed by defects in the formation of stable joint molecules. We suggest that Srs2, by limiting Rad51 accumulation on DNA, prevents the formation of aberrant recombination intermediates that otherwise would persist and interfere with normal chromosome segregation and nuclear division.

scholarly journals Discrimination against RNA Backbones by a ssDNA Binding Protein

Structure ◽  
2018 ◽  
Vol 26 (5) ◽  
pp. 722-733.e2 ◽  
Author(s):  
Neil R. Lloyd ◽  
Deborah S. Wuttke
Keyword(s):  
Binding Protein ◽  
Ssdna Binding ◽  
Ssdna Binding Protein

scholarly journals Crystal Structure of INTS3/INTS6 complex reveals Functional Importance of INTS3 dimerization in DSB Repair

2020 ◽  
Author(s):  
Yu Jia ◽  
Zixiu Cheng ◽  
Sakshibeedu R Bharath ◽  
Qiangzu Sun ◽  
Nannan Su ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Critical Role ◽  
Repair Process ◽  
Dsb Repair ◽  
Ssdna Binding ◽  
C Terminus ◽  
Ssdna Binding Protein ◽  
Direct Binding ◽  
Biochemical Analyses

AbstractSOSS1 is a single-stranded DNA (ssDNA)-binding protein complex that plays a critical role in double-strand DNA break (DSB) repair. SOSS1 consists of three subunits: INTS3, SOSSC, and hSSB1 with INTS3 serving as a scaffold to stabilize this complex. Moreover, the integrator complex subunit 6 (INTS6) participates in the DNA damage response through direct binding to INTS3 but how INTS3 interacts with INTS6 thereby, impacting DBS repair is not clear. Here, we determined the crystal structure of the C-terminus of INTS3 (INTS3c) in complex with the C-terminus of INTS6 (INTS6c) at a resolution of 2.4 Å. Structure analysis revealed that two INTS3c subunits dimerize and interact with INTS6c via conserved residues. Subsequent biochemical analyses confirmed that INTS3c forms a stable dimer and INTS3 dimerization is important for recognizing the longer ssDNA. Perturbation of INTS3c dimerization and disruption of the INTS3c/INTS6c interaction, impair the DSB repair process. Altogether, these results unravel the underappreciated role of INTS3 dimerization and the molecular basis of INTS3/INTS6 interaction in DSB repair.

scholarly journals Overexpression, purification and helix-destabilizing properties of Epstein-Barr virus ssDNA-binding protein.

1998 ◽  
Vol 79 (5) ◽  
pp. 1257-1264 ◽  
Author(s):  
T Tsurumi ◽  
N Yokoyama ◽  
Y Yamashita ◽  
J Kishore ◽  
H Yamada ◽  
...  
Keyword(s):  
Epstein Barr Virus ◽  
Binding Protein ◽  
Ssdna Binding ◽  
Barr Virus ◽  
Ssdna Binding Protein ◽  
Epstein Barr
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