APM OpenIR
Structural insight into the length-dependent binding of ssDNA by SP_0782 from Streptococcus pneumoniae, reveals a divergence in the DNA-binding interface of PC4-like proteins
Li, Shuangli1; Lu, Guoliang2,3,6; Fang, Xiang2,3; Ramelot, Theresa A.4,5; Kennedy, Michael A.4,5; Zhou, Xin1; Gong, Peng2; Zhang, Xu1; Liu, Maili1; Zhu, Jiang1; Yang, Yunhuang1
2020-01-10
Source PublicationNUCLEIC ACIDS RESEARCH
ISSN0305-1048
Volume48Issue:1Pages:432-444
AbstractSP_0782 from Streptococcus pneumoniae is a dimeric protein that potentially binds with single-stranded DNA (ssDNA) in a manner similar to human PC4, the prototype of PC4-like proteins, which plays roles in transcription and maintenance of genome stability. In a previous NMR study, SP_0782 exhibited an ssDNA-binding property different from YdbC, a prokaryotic PC4-like protein from Lactococcus lac-tis, but the underlying mechanism remains unclear. Here, we show that although SP_0782 adopts an overall fold similar to those of PC4 and YdbC, the ssDNA length occupied by SP_0782 is shorter than those occupied by PC4 and YdbC. SP_0782 exhibits varied binding patterns for different lengths of ssDNA, and tends to form large complexes with ssDNA in a potential high-density binding manner. The structures of SP_0782 complexed with different ssD-NAs reveal that the varied binding patterns are associated with distinct capture of nucleotides in two major DNA-binding regions of SP_0782. Moreover, a comparison of known structures of PC4-like proteins complexed with ssDNA reveals a divergence in the binding interface between prokaryotic and eukaryotic PC4-like proteins. This study provides insights into the ssDNA-binding mechanism of PC4-like proteins, and benefits further study regarding the biological function of SP_0782, probably in DNA protection and natural transformation.
Funding OrganizationNational Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; National Institute of General Medical Sciences of USA ; National Institute of General Medical Sciences of USA ; National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; National Institute of General Medical Sciences of USA ; National Institute of General Medical Sciences of USA ; National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; National Institute of General Medical Sciences of USA ; National Institute of General Medical Sciences of USA ; National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; National Institute of General Medical Sciences of USA ; National Institute of General Medical Sciences of USA
DOI10.1093/nar/gkz1045
WOS KeywordC-TERMINAL DOMAIN ; PC4 ; TRANSCRIPTION ; NMR ; SSB ; TRANSFORMATION ; RECOGNITION ; COMPETENCE ; HOMOLOG ; STRANDS
Language英语
Funding ProjectNational Key R&D Program of China[2016YFA051201] ; National Key R&D Program of China[2018YFA0507200] ; National Natural Sciences Foundation of China[21575155] ; National Natural Sciences Foundation of China[31670154] ; National Natural Sciences Foundation of China[31802147] ; National Institute of General Medical Sciences of USA[U54GM094597]
Funding OrganizationNational Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; National Institute of General Medical Sciences of USA ; National Institute of General Medical Sciences of USA ; National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; National Institute of General Medical Sciences of USA ; National Institute of General Medical Sciences of USA ; National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; National Institute of General Medical Sciences of USA ; National Institute of General Medical Sciences of USA ; National Key R&D Program of China ; National Key R&D Program of China ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; National Institute of General Medical Sciences of USA ; National Institute of General Medical Sciences of USA
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS IDWOS:000524741700037
PublisherOXFORD UNIV PRESS
Citation statistics
Document Type期刊论文
Identifierhttp://ir.apm.ac.cn/handle/112942/22493
Collection中国科学院武汉物理与数学研究所
Corresponding AuthorZhu, Jiang; Yang, Yunhuang
Affiliation1.Chinese Acad Sci, State Key Lab Magnet Resonance & Atom Mol Phys, Key Lab Magnet Resonance Biol Syst,Wuhan Natl Lab, Natl Ctr Magnet Resonance Wuhan,Wuhan Inst Phys &, Wuhan 430071, Peoples R China
2.Chinese Acad Sci, Key Lab Special Pathogens & Biosafety, Wuhan Inst Virol, Ctr Biosafety Mega Sci, Wuhan 430071, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.Miami Univ, Dept Chem & Biochem, Oxford, OH 45056 USA
5.Miami Univ, Northeast Struct Genom Consortium, Oxford, OH 45056 USA
6.Fudan Univ, Sch Life Sci, Shanghai 200438, Peoples R China
Recommended Citation
GB/T 7714
Li, Shuangli,Lu, Guoliang,Fang, Xiang,et al. Structural insight into the length-dependent binding of ssDNA by SP_0782 from Streptococcus pneumoniae, reveals a divergence in the DNA-binding interface of PC4-like proteins[J]. NUCLEIC ACIDS RESEARCH,2020,48(1):432-444.
APA Li, Shuangli.,Lu, Guoliang.,Fang, Xiang.,Ramelot, Theresa A..,Kennedy, Michael A..,...&Yang, Yunhuang.(2020).Structural insight into the length-dependent binding of ssDNA by SP_0782 from Streptococcus pneumoniae, reveals a divergence in the DNA-binding interface of PC4-like proteins.NUCLEIC ACIDS RESEARCH,48(1),432-444.
MLA Li, Shuangli,et al."Structural insight into the length-dependent binding of ssDNA by SP_0782 from Streptococcus pneumoniae, reveals a divergence in the DNA-binding interface of PC4-like proteins".NUCLEIC ACIDS RESEARCH 48.1(2020):432-444.
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