Evidence map›Paper›PMID 40296718›Full record

ArticleActa biochimica et biophysica Sinica2025

New feature of hMEIOB and hSPATA22 binding to ssDNA from a single-molecule perspective.

Yating Xu, Wei Qu, Erchi Zhou, Qi Sun, Weihao Gong, Lei Xu, Yaoke Lei, Zhangying Jia, Hanqing Shi, Xinghua Zhang and 1 more

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Article in Acta biochimica et biophysica Sinica, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

11 authors.

Yating XuState Key Laboratory of Metabolism and Regulation in Complex Organisms, Hubei Provincial Key Laboratory of Developmentally Originated Disease, TaiKang Center for Life and Medical Sciences, School of Basic Medical Sciences, Wuhan University, Wuhan 430072, China.
Wei QuReproductive Medicine Center, the Third Affiliated Hospital of Zhengzhou University, Zhengzhou 450052, China.
Erchi ZhouThe Institute for Advanced Studies, College of Life Sciences, State Key Laboratory of Virology, Hubei Key Laboratory of Cell Homeostasis, Wuhan University, Wuhan 430072, China.
Qi SunState Key Laboratory of Metabolism and Regulation in Complex Organisms, Hubei Provincial Key Laboratory of Developmentally Originated Disease, TaiKang Center for Life and Medical Sciences, School of Basic Medical Sciences, Wuhan University, Wuhan 430072, China.
Weihao GongState Key Laboratory of Metabolism and Regulation in Complex Organisms, Hubei Provincial Key Laboratory of Developmentally Originated Disease, TaiKang Center for Life and Medical Sciences, School of Basic Medical Sciences, Wuhan University, Wuhan 430072, China.
Lei XuState Key Laboratory of Metabolism and Regulation in Complex Organisms, Hubei Provincial Key Laboratory of Developmentally Originated Disease, TaiKang Center for Life and Medical Sciences, School of Basic Medical Sciences, Wuhan University, Wuhan 430072, China.
Yaoke LeiState Key Laboratory of Metabolism and Regulation in Complex Organisms, Hubei Provincial Key Laboratory of Developmentally Originated Disease, TaiKang Center for Life and Medical Sciences, School of Basic Medical Sciences, Wuhan University, Wuhan 430072, China.
Zhangying JiaState Key Laboratory of Metabolism and Regulation in Complex Organisms, Hubei Provincial Key Laboratory of Developmentally Originated Disease, TaiKang Center for Life and Medical Sciences, School of Basic Medical Sciences, Wuhan University, Wuhan 430072, China.
Hanqing ShiDepartment of Pathology, Renmin Hospital of Wuhan University, Wuhan 430072, China.
Xinghua ZhangReproductive Medicine Center, the Third Affiliated Hospital of Zhengzhou University, Zhengzhou 450052, China.
Mengcheng LuoState Key Laboratory of Metabolism and Regulation in Complex Organisms, Hubei Provincial Key Laboratory of Developmentally Originated Disease, TaiKang Center for Life and Medical Sciences, School of Basic Medical Sciences, Wuhan University, Wuhan 430072, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MEIOB and SPATA22 are gonad-specific proteins that function in meiosis recombination. Mutations in these two proteins cause oligospermia or azoospermia in human males. It has been reported that the heterodimer composed of MEIOB and SPATA22 recognizes and binds to the single-strand DNA (ssDNA) protected by the replication protein A (RPA) complex to promote DNA damage repair during homologous recombination. However, the amino acid sequences of the two proteins are inconsistent in humans and rodents, which leads to functional differences in meiosis. In this study, human-derived MEIOB (hMEIOB) and SPATA22 (hSPATA22) are expressed and purified for electrophoretic mobility shift assay (EMSA), magnetic tweezer (MT) assay and bio-layer interferometry (BLI) assay to analyze the ssDNA binding patterns. The results show that hMEIOB has low ssDNA-binding affinity and stability alone, but hSPATA22 binds to ssDNA faster and more stably and promotes ssDNA condensation. Strong binding affinity and stability to ssDNA are present when the hMEIOB-hSPATA22 heterodimer is formed. Moreover, we find that multiple hMEIOB-hSPATA22 heterodimers spontaneously aggregate

Indexed as

Cell Cycle ProteinsDNA-Binding ProteinsDNA, Single-StrandedHumansProtein BindingProtein MultimerizationReplication Protein ACell Cycle ProteinsDNA-Binding ProteinsDNA, Single-StrandedReplication Protein Abio-layer interferometry.heterodimermagnetic tweezerMEIOBSPATA22ssDNA

Identifiers

PMID40296718
PMCPMC12666670

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.