scholarly journals SYCE2 is required for synaptonemal complex assembly, double strand break repair, and homologous recombination

2007 ◽  
Vol 176 (6) ◽  
pp. 741-747 ◽  
Author(s):  
Ewelina Bolcun-Filas ◽  
Yael Costa ◽  
Robert Speed ◽  
Mary Taggart ◽  
Ricardo Benavente ◽  
...  
Keyword(s):  
Homologous Recombination ◽  
Synaptonemal Complex ◽  
Protein Interactions ◽  
Central Element ◽  
Strand Break ◽  
Protein Protein Interactions ◽  
Dna Breakage ◽  
Paired Chromosome ◽  
Meiotic Chromosomes ◽  
Males And Females

Synapsis is the process by which paired chromosome homologues closely associate in meiosis before crossover. In the synaptonemal complex (SC), axial elements of each homologue connect through molecules of SYCP1 to the central element, which contains the proteins SYCE1 and -2. We have derived mice lacking SYCE2 protein, producing males and females in which meiotic chromosomes align and axes form but do not synapse. Sex chromosomes are unaligned, not forming a sex body. Additionally, markers of DNA breakage and repair are retained on the axes, and crossover is impaired, culminating in both males and females failing to produce gametes. We show that SC formation can initiate at sites of SYCE1/SYCP1 localization but that these points of initiation cannot be extended in the absence of SYCE2. SC assembly is thus dependent on SYCP1, SYCE1, and SYCE2. We provide a model to explain this based on protein–protein interactions.

scholarly journals ZmRAD51C Is Essential for Double-Strand Break Repair and Homologous Recombination in Maize Meiosis

2019 ◽  
Vol 20 (21) ◽  
pp. 5513 ◽  
Author(s):  
Juli Jing ◽  
Ting Zhang ◽  
Yazhong Wang ◽  
Zhenhai Cui ◽  
Yan He
Keyword(s):  
Homologous Recombination ◽  
Early Stage ◽  
Central Element ◽  
Strand Break ◽  
Double Strand Break ◽  
Dsb Repair ◽  
Homologous Chromosomes ◽  
Meiotic Chromosomes ◽  
Homologous Chromosome Pairing ◽  
Axial Element

Radiation sensitive 51 (RAD51) recombinases play crucial roles in meiotic double-strand break (DSB) repair mediated by homologous recombination (HR) to ensure the correct segregation of homologous chromosomes. In this study, we identified the meiotic functions of ZmRAD51C, the maize homolog of Arabidopsis and rice RAD51C. The Zmrad51c mutants exhibited regular vegetative growth but complete sterility for both male and female inflorescence. However, the mutants showed hypersensitivity to DNA damage by mitomycin C. Cytological analysis indicated that homologous chromosome pairing and synapsis were rigorously inhibited, and meiotic chromosomes were often entangled from diplotene to metaphase I, leading to chromosome fragmentation at anaphase I. Immunofluorescence analysis showed that although the signals of the axial element absence of first division (AFD1) and asynaptic1 (ASY1) were normal, the assembly of the central element zipper1 (ZYP1) was severely disrupted. The DSB formation was normal in Zmrad51c meiocytes, symbolized by the regular occurrence of γH2AX signals. However, RAD51 and disrupted meiotic cDNA 1 (DMC1) signals were never detected at the early stage of prophase I in the mutant. Taken together, our results indicate that ZmRAD51C functions crucially for both meiotic DSB repair and homologous recombination in maize.

scholarly journals Conservation and Variability of Synaptonemal Complex Proteins in Phylogenesis of Eukaryotes

2014 ◽  
Vol 2014 ◽  
pp. 1-16 ◽  
Author(s):  
Tatiana M. Grishaeva ◽  
Yuri F. Bogdanov
Keyword(s):  
Synaptonemal Complex ◽  
Protein Interactions ◽  
Phylogenetic Trees ◽  
Flowering Plants ◽  
Model Organisms ◽  
Protein Protein Interactions ◽  
Lateral Element ◽  
Origin And Evolution ◽  
Eukaryotic Proteomes ◽  
Related Proteins

The problems of the origin and evolution of meiosis include the enigmatic variability of the synaptonemal complexes (SCs) which, being morphology similar, consist of different proteins in different eukaryotic phyla. Using bioinformatics methods, we monitored all available eukaryotic proteomes to find proteins similar to known SC proteins of model organisms. We found proteins similar to SC lateral element (LE) proteins and possessing the HORMA domain in the majority of the eukaryotic taxa and assume them the most ancient among all SC proteins. Vertebrate LE proteins SYCP2, SYCP3, and SC65 proved to have related proteins in many invertebrate taxa. Proteins of SC central space are most evolutionarily variable. It means that different protein-protein interactions can exist to connect LEs. Proteins similar to the known SC proteins were not found in Euglenophyta, Chrysophyta, Charophyta, Xanthophyta, Dinoflagellata, and primitive Coelomata. We conclude that different proteins whose common feature is the presence of domains with a certain conformation are involved in the formation of the SC in different eukaryotic phyla. This permits a targeted search for orthologs of the SC proteins using phylogenetic trees. Here we consider example of phylogenetic trees for protozoans, fungi, algae, mosses, and flowering plants.

scholarly journals Rad51 and Dmc1 Form Mixed Complexes Associated with Mouse Meiotic Chromosome Cores and Synaptonemal Complexes

1999 ◽  
Vol 147 (2) ◽  
pp. 207-220 ◽  
Author(s):  
Madalena Tarsounas ◽  
Takashi Morita ◽  
Ronald E. Pearlman ◽  
Peter B. Moens
Keyword(s):  
Protein Interactions ◽  
Meiotic Chromosome ◽  
Amino Acid Level ◽  
Distribution Patterns ◽  
Early Prophase ◽  
Protein Protein Interactions ◽  
Prophase I ◽  
Meiotic Chromosomes ◽  
Yeast Meiosis

The eukaryotic RecA homologues RAD51 and DMC1 function in homology recognition and formation of joint-molecule recombination intermediates during yeast meiosis. The precise immunolocalization of these two proteins on the meiotic chromosomes of plants and animals has been complicated by their high degree of identity at the amino acid level. With antibodies that have been immunodepleted of cross-reactive epitopes, we demonstrate that RAD51 and DMC1 have identical distribution patterns in extracts of mouse spermatocytes in successive prophase I stages, suggesting coordinate functionality. Immunofluorescence and immunoelectron microscopy with these antibodies demonstrate colocalization of the two proteins on the meiotic chromosome cores at early prophase I. We also show that mouse RAD51 and DMC1 establish protein–protein interactions with each other and with the chromosome core component COR1(SCP3) in a two-hybrid system and in vitro binding analyses. These results suggest that the formation of a multiprotein recombination complex associated with the meiotic chromosome cores is essential for the development and fulfillment of the meiotic recombination process.

scholarly journals Beyond reversal: ubiquitin and ubiquitin-like proteases and the orchestration of the DNA double strand break repair response

2019 ◽  
Vol 47 (6) ◽  
pp. 1881-1893
Author(s):  
Alexander J. Garvin
Keyword(s):  
Protein Interactions ◽  
Cellular Response ◽  
Strand Break ◽  
Central Component ◽  
Protein Protein Interactions ◽  
Dna Double Strand Breaks ◽  
Dsb Repair ◽  
Post Translational Modifications ◽  
Strand Breaks ◽  
Dna Double Strand Break

The cellular response to genotoxic DNA double strand breaks (DSBs) uses a multitude of post-translational modifications to localise, modulate and ultimately clear DNA repair factors in a timely and accurate manner. Ubiquitination is well established as vital to the DSB response, with a carefully co-ordinated pathway of histone ubiquitination events being a central component of DSB signalling. Other ubiquitin-like modifiers (Ubl) including SUMO and NEDD8 have since been identified as playing important roles in DSB repair. In the last five years ∼20 additional Ub/Ubl proteases have been implicated in the DSB response. The number of proteases identified highlights the complexity of the Ub/Ubl signal present at DSBs. Ub/Ubl proteases regulate turnover, activity and protein–protein interactions of DSB repair factors both catalytically and non-catalytically. This not only ensures efficient repair of breaks but has a role in channelling repair into the correct DSB repair sub-pathways. Ultimately Ub/Ubl proteases have essential roles in maintaining genomic stability. Given that deficiencies in many Ub/Ubl proteases promotes sensitivity to DNA damaging chemotherapies, they could be attractive targets for cancer treatment.

Protein-protein interactions in the yeast pheromone response pathway: Ste5p interacts with all members of the MAP kinase cascade.

Genetics ◽  
1994 ◽  
Vol 138 (3) ◽  
pp. 609-619 ◽  
Author(s):  
J A Printen ◽  
G F Sprague
Keyword(s):  
Map Kinase ◽  
Protein Interactions ◽  
Map Kinases ◽  
Central Element ◽  
Signal Propagation ◽  
Protein Protein Interactions ◽  
Pheromone Response ◽  
Pheromone Response Pathway ◽  
Map Kinase Cascade ◽  
Kinase Cascade

Abstract We have used the two-hybrid system of Fields and Song to identify protein-protein interactions that occur in the pheromone response pathway of the yeast Saccharomyces cerevisiae. Pathway components Ste4p, Ste5p, Ste7p, Ste11p, Ste12p, Ste20p, Fus3p and Kss1p were tested in all pairwise combinations. All of the interactions we detected involved at least one member of the MAP kinase cascade that is a central element of the response pathway. Ste5p, a protein of unknown biochemical function, interacted with protein kinases that operate at each step of the MAP kinase cascade, specifically with Ste11p (an MEKK), Ste7p (an MEK), and Fus3p (a MAP kinase). This finding suggests that one role of Ste5p is to serve as a scaffold to facilitate interactions among members of the kinase cascade. In this role as facilitator, Ste5p may make both signal propagation and signal attenuation more efficient. Ste5p may also help minimize cross-talk with other MAP kinase cascades and thus ensure the integrity of the pheromone response pathway. We also found that both Ste11p and Ste7p interact with Fus3p and Kss1p. Finally, we detected an interaction between one of the MAP kinases, Kss1p, and a presumptive target, the transcription factor Ste12p. We failed to detect interactions of Ste4p or Ste20p with any other component of the response pathway.

scholarly journals Protein-protein interactions in the synaptonemal complex.

1997 ◽  
Vol 8 (8) ◽  
pp. 1405-1414 ◽  
Author(s):  
M Tarsounas ◽  
R E Pearlman ◽  
P J Gasser ◽  
M S Park ◽  
P B Moens
Keyword(s):  
Synaptonemal Complex ◽  
Protein Interactions ◽  
Coiled Coil ◽  
Protein Protein Interactions ◽  
Late Prophase ◽  
Yeast Saccharomyces Cerevisiae ◽  
Heterotypic Interactions ◽  
Two Hybrid ◽  
Homotypic Interactions

In mammalian systems, an approximately M(r) 30,000 Cor1 protein has been identified as a major component of the meiotic prophase chromosome cores, and a M(r) 125,000 Syn1 protein is present between homologue cores where they are synapsed and form the synaptonemal complex (SC). Immunolocalization of these proteins during meiosis suggests possible homo- and heterotypic interactions between the two as well as possible interactions with yet unrecognized proteins. We used the two-hybrid system in the yeast Saccharomyces cerevisiae to detect possible protein-protein associations. Segments of hamsters Cor1 and Syn1 proteins were tested in various combinations for homo- and heterotypic interactions. In the cause of Cor1, homotypic interactions involve regions capable of coiled-coil formation, observation confirmed by in vitro affinity coprecipitation experiments. The two-hybrid assay detects no interaction of Cor1 protein with central and C-terminal fragments of Syn1 protein and no homotypic interactions involving these fragments of Syn1. Hamster Cor1 and Syn1 proteins both associate with the human ubiquitin-conjugation enzyme Hsubc9 as well as with the hamster Ubc9 homologue. The interactions between SC proteins and the Ubc9 protein may be significant for SC disassembly, which coincides with the repulsion of homologs by late prophase I, and also for the termination of sister centromere cohesiveness at anaphase II.

scholarly journals SUMO Localizes to the Central Element of Synaptonemal Complex and Is Required for the Full Synapsis of Meiotic Chromosomes in Budding Yeast

PLoS Genetics ◽  
2013 ◽  
Vol 9 (10) ◽  
pp. e1003837 ◽  
Author(s):  
Karen Voelkel-Meiman ◽  
Louis F. Taylor ◽  
Pritam Mukherjee ◽  
Neil Humphryes ◽  
Hideo Tsubouchi ◽  
...  
Keyword(s):  
Synaptonemal Complex ◽  
Budding Yeast ◽  
Central Element ◽  
Meiotic Chromosomes

scholarly journals The Cohesin Complex and Its Interplay with Non-Coding RNAs

2021 ◽  
Vol 7 (4) ◽  
pp. 67
Author(s):  
Merve Kuru-Schors ◽  
Monika Haemmerle ◽  
Tony Gutschner
Keyword(s):  
Gene Expression ◽  
Protein Interactions ◽  
Strand Break ◽  
Cohesin Complex ◽  
Protein Protein Interactions ◽  
Chromosome Architecture ◽  
Dna Double Strand Break ◽  
Chromatid Cohesion ◽  
Dna Modifications ◽  
Non Coding Rnas

The cohesin complex is a multi-subunit protein complex initially discovered for its role in sister chromatid cohesion. However, cohesin also has several other functions and plays important roles in transcriptional regulation, DNA double strand break repair, and chromosome architecture thereby influencing gene expression and development in organisms from yeast to man. While most of these functions rely on protein–protein interactions, post-translational protein, as well as DNA modifications, non-coding RNAs are emerging as additional players that facilitate and modulate the function or expression of cohesin and its individual components. This review provides a condensed overview about the architecture as well as the function of the cohesin complex and highlights its multifaceted interplay with both short and long non-coding RNAs.

scholarly journals PAIR3, an axis-associated protein, is essential for the recruitment of recombination elements onto meiotic chromosomes in rice

2011 ◽  
Vol 22 (1) ◽  
pp. 12-19 ◽  
Author(s):  
Kejian Wang ◽  
Mo Wang ◽  
Ding Tang ◽  
Yi Shen ◽  
Baoxiang Qin ◽  
...  
Keyword(s):  
Synaptonemal Complex ◽  
Central Element ◽  
Dependent Manner ◽  
Homologous Pairing ◽  
Homologous Chromosomes ◽  
Prophase I ◽  
Meiotic Chromosomes

During meiosis, the paired homologous chromosomes are tightly held together by the synaptonemal complex (SC). This complex consists of two parallel axial/lateral elements (AEs/LEs) and one central element. Here, we observed that PAIR3 localized to the chromosome core during prophase I and associated with both unsynapsed AEs and synapsed LEs. Analyses of the severe pair3 mutant demonstrated that PAIR3 was essential for bouquet formation, homologous pairing and normal recombination, and SC assembly. In addition, we showed that although PAIR3 was not required for the initial recruitment of PAIR2, it was required for the proper association of PAIR2 with chromosomes. Dual immunostaining revealed that PAIR3 highly colocalized with REC8. Moreover, studies using a rec8 mutant indicated that PAIR3 localized to chromosomes in a REC8-dependent manner.

Sign in / Sign up

Export Citation Format

Share Document