A meiotic XPF–ERCC1-like complex recognizes joint molecule recombination intermediates to promote crossover formation
Published 2018 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
A meiotic XPF–ERCC1-like complex recognizes joint molecule recombination intermediates to promote crossover formation
Authors
Keywords
-
Journal
GENES & DEVELOPMENT
Volume 32, Issue 3-4, Pages 283-296
Publisher
Cold Spring Harbor Laboratory
Online
2018-02-10
DOI
10.1101/gad.308510.117
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Physiological protein blocks direct the Mre11–Rad50–Xrs2 and Sae2 nuclease complex to initiate DNA end resection
- (2017) Giordano Reginato et al. GENES & DEVELOPMENT
- Control of structure-specific endonucleases to maintain genome stability
- (2017) Pierre-Marie Dehé et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Functions and regulation of the multitasking FANCM family of DNA motor proteins
- (2015) Xiaoyu Xue et al. GENES & DEVELOPMENT
- Top3-Rmi1 DNA Single-Strand Decatenase Is Integral to the Formation and Resolution of Meiotic Recombination Intermediates
- (2015) Hardeep Kaur et al. MOLECULAR CELL
- Pervasive and Essential Roles of the Top3-Rmi1 Decatenase Orchestrate Recombination and Facilitate Chromosome Segregation in Meiosis
- (2015) Shangming Tang et al. MOLECULAR CELL
- Phosphorylation of the Synaptonemal Complex Protein Zip1 Regulates the Crossover/Noncrossover Decision during Yeast Meiosis
- (2015) Xiangyu Chen et al. PLOS BIOLOGY
- Transcription dynamically patterns the meiotic chromosome-axis interface
- (2015) Xiaoji Sun et al. eLife
- Crystal structure of a Fanconi anemia-associated nuclease homolog bound to 5′ flap DNA: basis of interstrand cross-link repair by FAN1
- (2014) Gwang Hyeon Gwon et al. GENES & DEVELOPMENT
- TheSaccharomyces cerevisiaeMlh1-Mlh3 Heterodimer Is an Endonuclease That Preferentially Binds to Holliday Junctions
- (2014) Lepakshi Ranjha et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Antagonistic roles of ubiquitin ligase HEI10 and SUMO ligase RNF212 regulate meiotic recombination
- (2014) Huanyu Qiao et al. NATURE GENETICS
- bPeaks: a bioinformatics tool to detect transcription factor binding sites from ChIPseq data in yeasts and other organisms with small genomes
- (2014) Jawad Merhej et al. YEAST
- Correction: Controlling Meiotic Recombinational Repair – Specifying the Roles of ZMMs, Sgs1 and Mus81/Mms4 in Crossover Formation
- (2014) PLoS Genetics
- RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis
- (2013) April Reynolds et al. NATURE GENETICS
- Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity
- (2013) M. Levikova et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Pch2 is a hexameric ring ATPase that remodels the chromosome axis protein Hop1
- (2013) C. Chen et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Architecture and DNA Recognition Elements of the Fanconi Anemia FANCM-FAAP24 Complex
- (2013) Rachel Coulthard et al. STRUCTURE
- High-Resolution Comparative Modeling with RosettaCM
- (2013) Yifan Song et al. STRUCTURE
- Differential Association of the Conserved SUMO Ligase Zip3 with Meiotic Double-Strand Break Sites Reveals Regional Variations in the Outcome of Meiotic Recombination
- (2013) Maria-Elisabetta Serrentino et al. PLoS Genetics
- Delineation of Joint Molecule Resolution Pathways in Meiosis Identifies a Crossover-Specific Resolvase
- (2012) Kseniya Zakharyevich et al. CELL
- Protein Group Modification and Synergy in the SUMO Pathway as Exemplified in DNA Repair
- (2012) Ivan Psakhye et al. CELL
- BLM Helicase Ortholog Sgs1 Is a Central Regulator of Meiotic Recombination Intermediate Metabolism
- (2012) Arnaud De Muyt et al. MOLECULAR CELL
- Structural and Functional Discussion of the Tetra-Trico-Peptide Repeat, a Protein Interaction Module
- (2012) Natalie Zeytuni et al. STRUCTURE
- Spo11-Accessory Proteins Link Double-Strand Break Sites to the Chromosome Axis in Early Meiotic Recombination
- (2011) Silvia Panizza et al. CELL
- SHOC1 and PTD form an XPF-ERCC1-like complex that is required for formation of class I crossovers
- (2011) N. Macaisne et al. JOURNAL OF CELL SCIENCE
- HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment
- (2011) Michael Remmert et al. NATURE METHODS
- The Fanconi Anemia Protein, FANCG, Binds to the ERCC1-XPF Endonuclease via Its Tetratricopeptide Repeats and the Central Domain of ERCC1
- (2010) Chuan Wang et al. BIOCHEMISTRY
- Recombination Proteins Mediate Meiotic Spatial Chromosome Organization and Pairing
- (2010) Aurora Storlazzi et al. CELL
- Ultrafast and memory-efficient alignment of short DNA sequences to the human genome
- (2009) Ben Langmead et al. GENOME BIOLOGY
- Structural and Functional Relationships of the XPF/MUS81 Family of Proteins
- (2008) Alberto Ciccia et al. Annual Review of Biochemistry
- SHOC1, an XPF Endonuclease-Related Protein, Is Essential for the Formation of Class I Meiotic Crossovers
- (2008) Nicolas Macaisne et al. CURRENT BIOLOGY
- Initiation of meiotic chromosome synapsis at centromeres in budding yeast
- (2008) T. Tsubouchi et al. GENES & DEVELOPMENT
- Meiotic failure in male mice lacking an X-linked factor
- (2008) F. Yang et al. GENES & DEVELOPMENT
- Cdc7-dependent phosphorylation of Mer2 facilitates initiation of yeast meiotic recombination
- (2008) H. Sasanuma et al. GENES & DEVELOPMENT
- Rad52 Promotes Postinvasion Steps of Meiotic Double-Strand-Break Repair
- (2008) Jessica P. Lao et al. MOLECULAR CELL
- Crossover assurance and crossover interference are distinctly regulated by the ZMM proteins during yeast meiosis
- (2008) Miki Shinohara et al. NATURE GENETICS
Add your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started