Crystal structure of Hop2–Mnd1 and mechanistic insights into its role in meiotic recombination

Kang, Hyung Seok; Shin, Hang‐Sik; Kalantzi, Alexandra-Styliani; Toseland, Christopher P.; Kim, Hyunmin; Gruber, Stephan; Peraro, Matteo Dal; Oh, Byung‐Ha

doi:10.1093/nar/gkv172

Cited by 47 publications

(69 citation statements)

References 59 publications

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“…3). Furthermore, through implementation of the iterative comparative modeling approach described here, the structure of a dominant open conformation of the protein was predicted, which is similar to a crystal structure of the related HOP2–MND1 complex from Giardia lamblia 8,47. Interestingly, our data also suggested a co-existing closed conformation that was not captured during XRC analysis of the related complex.…”

Section: Introductionsupporting

confidence: 60%

Structural prediction of protein models using distance restraints derived from cross-linking mass spectrometry data

et al. 2018

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This protocol describes a workflow for creating structural models of proteins or protein complexes using distance restraints derived from cross-linking mass spectrometry experiments. The distance restraints are used (i) to adjust preliminary models that are calculated based on a homologous template and primary sequence and (ii) to select the model that is in best agreement with the experimental data. In the case of protein complexes, the cross-linking data is further used to dock the subunits to one another to generate models of the interacting proteins. Predicting models in such a manner has the potential to indicate multiple conformations and dynamic changes that occur in solution. This modeling protocol is compatible with many cross-linking workflows and uses open-source programs or programs that are free for academic users and do not require expertise in computational modeling. This protocol is an excellent additional application with which to use cross-linking results for building structural models of proteins. The established protocol is expected to take 6-12 days to complete, depending on the size of the proteins and the complexity of the cross-linking data.

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Section: Introductionsupporting

confidence: 60%

Structural prediction of protein models using distance restraints derived from cross-linking mass spectrometry data

et al. 2018

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“…; Kang et al . ), also share structural similarity with SYCP3. It will be intriguing to determine whether these Rad51 activators compete with the yeast SYCP3 analogue.…”

Section: Discussionmentioning

confidence: 88%

“…HOP2‐MND1 forms a coiled‐coil structure, which is structurally similar to the SYCP3 filament (Kang et al . ). Other Rad51 activators, such as the Schizosaccharomyces pombe Swi5‐Sfr1 complex and the S. cerevisiae Mei5‐Sae3 complex (Hayase et al .…”

Section: Discussionmentioning

confidence: 97%

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SYCP3 regulates strand invasion activities of RAD51 and DMC1

et al. 2017

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The synaptonemal complex is a higher-ordered proteinaceous architecture formed between homologous chromosomes. SYCP3 is a major component of the lateral/axial elements in the synaptonemal complex and is essential for meiotic recombination. Previous genetic studies showed that SYCP3 functions in meiotic homologous recombination biased to interhomologous chromosomes, by regulating the strand invasion activities of the RAD51 and DMC1 recombinases. However, the mechanism by which SYCP3 regulates RAD51- and DMC1-mediated strand invasion remains elusive. In this study, we found that SYCP3 significantly suppresses the RAD51-mediated, but not the DMC1-mediated, strand invasion reaction by competing with HOP2-MND1, which is an activator for both RAD51 and DMC1. A SYCP3 mutant with defective RAD51 binding does not inhibit the RAD51-mediated homologous recombination in human cells. Therefore, SYCP3 may promote the DMC1-driven homologous recombination by attenuating the RAD51 activity during meiosis.

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“…It encodes a 228‐amino acid (AAs) protein. According to the crystal structure (Kang et al ., ), OsHOP2 contains an N‐terminal winged‐helix domain (WHD) and three leucine zippers: LZ1, LZ2 and LZ3 (Fig. c).…”

Section: Resultsmentioning

confidence: 99%

OsHOP2 regulates the maturation of crossovers by promoting homologous pairing and synapsis in rice meiosis

et al. 2019

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Summary Meiotic recombination is closely linked with homologous pairing and synapsis. Previous studies have shown that HOMOLOGOUS PAIRING PROTEIN2 (HOP2), plays an essential role in homologous pairing and synapsis. However, the mechanism by which HOP2 regulates crossover (CO) formation has not been elucidated. Here, we show that OsHOP2 mediates the maturation of COs by promoting homologous pairing and synapsis in rice (Oryza sativa) meiosis. We used a combination of genetic analysis, immunolocalization and super‐resolution imaging to analyze the function of OsHOP2 in rice meiosis. We showed that full‐length pairing, synapsis and CO formation are disturbed in Oshop2 meiocytes. Moreover, structured illumination microscopy showed that OsHOP2 localized to chromatin and displayed considerable co‐localization with axial elements (AEs) and central elements (CEs). Importantly, the interaction between OsHOP2 and a transverse filament protein of synaptonemal complex (ZEP1), provided further evidence that OsHOP2 was involved in assembly or stabilization of the structure of the synaptonemal complex (SC). Although the initiation of recombination and CO designation occur normally in Oshop2 mutants, mature COs were severely reduced, and human enhancer of invasion 10 (HEI10)10 foci were only present on the synapsed region. Putting the data together, we speculate that OsHOP2 may serve as a global regulator to coordinate homologous pairing, synapsis and meiotic recombination in rice meiosis.

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Crystal structure of Hop2–Mnd1 and mechanistic insights into its role in meiotic recombination

Cited by 47 publications

References 59 publications

Structural prediction of protein models using distance restraints derived from cross-linking mass spectrometry data

Structural prediction of protein models using distance restraints derived from cross-linking mass spectrometry data

SYCP3 regulates strand invasion activities of RAD51 and DMC1

OsHOP2 regulates the maturation of crossovers by promoting homologous pairing and synapsis in rice meiosis

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