scholarly journals Interlace between Chromatin Structure, DNA Repair and Ubiquitination

2018 ◽  
Author(s):  
Attya Bhatti ◽  
Shanzay Ahmed ◽  
Arooma Jannat ◽  
Peter John
Keyword(s):  
Dna Repair ◽  
Chromatin Structure

scholarly journals A Role for Histone H2B During Repair of UV-Induced DNA Damage in Saccharomyces cerevisiae

Genetics ◽  
2002 ◽  
Vol 160 (4) ◽  
pp. 1375-1387
Author(s):  
Emmanuelle M D Martini ◽  
Scott Keeney ◽  
Mary Ann Osley
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Chromatin Structure ◽  
Specific Effect ◽  
Cell Killing ◽  
Cyclobutane Pyrimidine Dimers ◽  
Histone H2b ◽  
Uv Sensitivity ◽  
Pyrimidine Dimers

Abstract To investigate the role of the nucleosome during repair of DNA damage in yeast, we screened for histone H2B mutants that were sensitive to UV irradiation. We have isolated a new mutant, htb1-3, that shows preferential sensitivity to UV-C. There is no detectable difference in bulk chromatin structure or in the number of UV-induced cis-syn cyclobutane pyrimidine dimers (CPD) between HTB1 and htb1-3 strains. These results suggest a specific effect of this histone H2B mutation in UV-induced DNA repair processes rather than a global effect on chromatin structure. We analyzed the UV sensitivity of double mutants that contained the htb1-3 mutation and mutations in genes from each of the three epistasis groups of RAD genes. The htb1-3 mutation enhanced UV-induced cell killing in rad1Δ and rad52Δ mutants but not in rad6Δ or rad18Δ mutants, which are defective in postreplicational DNA repair (PRR). When combined with other mutations that affect PRR, the histone mutation increased the UV sensitivity of strains with defects in either the error-prone (rev1Δ) or error-free (rad30Δ) branches of PRR, but did not enhance the UV sensitivity of a strain with a rad5Δ mutation. When combined with a ubc13Δ mutation, which is also epistatic with rad5Δ, the htb1-3 mutation enhanced UV-induced cell killing. These results suggest that histone H2B acts in a novel RAD5-dependent branch of PRR.

scholarly journals Crystal structure of the ATPase-C domain of the chromatin remodeller Fun30 fromSaccharomyces cerevisiae

2017 ◽  
Vol 73 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Lan Liu ◽  
Tao Jiang
Keyword(s):  
Crystal Structure ◽  
Dna Repair ◽  
Gene Silencing ◽  
Chromatin Structure ◽  
Family Members ◽  
Atpase Domain ◽  
Repair Gene ◽  
Dna Repair Gene

Fun30 (Function unknown now 30) is a chromatin remodeller belonging to the Snf2 family. It has previously been reported to be a regulator of several cellular activities, including DNA repair, gene silencing and maintenance of chromatin structure. Here, the crystal structure of the Fun30 ATPase-C domain (the C-lobe of the ATPase domain) is reported at 1.95 Å resolution. Although the structure displays overall similarities to those of other Snf2 family members, a new structural module was found to be specific to the Fun30 subfamily. Fun30 ATPase-C was shown be monomeric in solution and showed no detectable affinity for dsDNA.

scholarly journals Essential histone chaperones collaborate to regulate transcription and chromatin integrity

2020 ◽  
Author(s):  
Olga Viktorovskaya ◽  
James Chuang ◽  
Dhawal Jain ◽  
Natalia I. Reim ◽  
Francheska López-Rivera ◽  
...  
Keyword(s):  
Dna Repair ◽  
Dna Replication ◽  
Chromatin Structure ◽  
Elongation Factor ◽  
Physical Interaction ◽  
Dependent Manner ◽  
Histone Chaperones ◽  
Transcription Elongation Factor ◽  
Nucleosome Organization ◽  
Chromatin Integrity

SUMMARYHistone chaperones are critical for controlling chromatin integrity during transcription, DNA replication, and DNA repair. We have discovered that the physical interaction between two essential histone chaperones, Spt6 and Spn1/Iws1, is required for transcriptional accuracy and nucleosome organization. To understand this requirement, we have isolated suppressors of an spt6 mutation that disrupts the Spt6-Spn1 interaction. Several suppressors are in a third essential histone chaperone, FACT, while another suppressor is in the transcription elongation factor Spt5/DSIF. The FACT suppressors weaken FACT-nucleosome interactions and bypass the requirement for Spn1, possibly by restoring a necessary balance between Spt6 and FACT on chromatin. In contrast, the Spt5 suppressor modulates Spt6 function in a Spn1-dependent manner. Despite these distinct mechanisms, both suppressors alleviate the nucleosome organization defects caused by disruption of the Spt6-Spn1 interaction. Taken together, we have uncovered a network in which histone chaperones and other elongation factors coordinate transcriptional integrity and chromatin structure.

scholarly journals DNA repair regulates chromatin structure and key transcription factors

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Benjamiin Snow ◽  
Todd Estabrook ◽  
De‐Sheng Pei ◽  
Phyllis R Strauss
Keyword(s):  
Dna Repair ◽  
Transcription Factors ◽  
Chromatin Structure

scholarly journals Correction: Chromatin structure, transcriptional activity and DNA repair efficiency affect the outcome of chemotherapy in multiple myeloma

2020 ◽  
Vol 122 (11) ◽  
pp. 1727-1728
Author(s):  
M. Gkotzamanidou ◽  
P. P. Sfikakis ◽  
S. A. Kyrtopoulos ◽  
C. Bamia ◽  
M. A. Dimopoulos ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
Dna Repair ◽  
Chromatin Structure ◽  
Transcriptional Activity ◽  
Repair Efficiency

Perfecting DNA double-strand break repair on transcribed chromatin

2020 ◽  
Vol 64 (5) ◽  
pp. 705-719 ◽  
Author(s):  
Xin Yi Tan ◽  
Michael S.Y. Huen
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Chromosomal Aberrations ◽  
Chromatin Structure ◽  
Genome Stability ◽  
Transcriptional Control ◽  
Strand Break ◽  
Double Strand Break ◽  
Dna Double Strand Break ◽  
Molecular Bases

Abstract Timely repair of DNA double-strand break (DSB) entails coordination with the local higher order chromatin structure and its transaction activities, including transcription. Recent studies are uncovering how DSBs trigger transient suppression of nearby transcription to permit faithful DNA repair, failing of which leads to elevated chromosomal aberrations and cell hypersensitivity to DNA damage. Here, we summarize the molecular bases for transcriptional control during DSB metabolism, and discuss how the exquisite coordination between the two DNA-templated processes may underlie maintenance of genome stability and cell homeostasis.

scholarly journals Single-molecule measurements reveal that PARP1 condenses DNA by loop stabilization

2021 ◽  
Vol 7 (33) ◽  
pp. eabf3641
Author(s):  
Nicholas A. W. Bell ◽  
Philip J. Haynes ◽  
Katharina Brunner ◽  
Taiana Maia de Oliveira ◽  
Maria M. Flocco ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Transcription Regulation ◽  
Single Molecule ◽  
Chromatin Structure ◽  
Parp Inhibitors ◽  
Chromatin Organization ◽  
Mechanical Forces ◽  
Dna Loops ◽  
Condensation Activity

Poly(ADP-ribose) polymerase 1 (PARP1) is an abundant nuclear enzyme that plays important roles in DNA repair, chromatin organization and transcription regulation. Although binding and activation of PARP1 by DNA damage sites has been extensively studied, little is known about how PARP1 binds to long stretches of undamaged DNA and how it could shape chromatin architecture. Here, using single-molecule techniques, we show that PARP1 binds and condenses undamaged, kilobase-length DNA subject to sub-piconewton mechanical forces. Stepwise decondensation at high force and DNA braiding experiments show that the condensation activity is due to the stabilization of DNA loops by PARP1. PARP inhibitors do not affect the level of condensation of undamaged DNA but act to block condensation reversal for damaged DNA in the presence of NAD+. Our findings suggest a mechanism for PARP1 in the organization of chromatin structure.

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