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6KUG

Crystal structure of YBX1 CSD with RNA

Summary for 6KUG
Entry DOI10.2210/pdb6kug/pdb
DescriptorNuclease-sensitive element-binding protein 1, RNA (5'-R(P*GP*CP*CP*U)-3') (3 entities in total)
Functional Keywordscsd, rna binding protein, rna binding protein-rna complex, rna binding protein/rna
Biological sourceHomo sapiens (Human)
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Total number of polymer chains2
Total formula weight9927.56
Authors
Zou, F.,Li, S. (deposition date: 2019-09-02, release date: 2020-02-05, Last modification date: 2024-03-27)
Primary citationZou, F.,Tu, R.,Duan, B.,Yang, Z.,Ping, Z.,Song, X.,Chen, S.,Price, A.,Li, H.,Scott, A.,Perera, A.,Li, S.,Xie, T.
DrosophilaYBX1 homolog YPS promotes ovarian germ line stem cell development by preferentially recognizing 5-methylcytosine RNAs.
Proc.Natl.Acad.Sci.USA, 117:3603-3609, 2020
Cited by
PubMed Abstract: 5-Methylcytosine (mC) is a RNA modification that exists in tRNAs and rRNAs and was recently found in mRNAs. Although it has been suggested to regulate diverse biological functions, whether mC RNA modification influences adult stem cell development remains undetermined. In this study, we show that Ypsilon schachtel (YPS), a homolog of human Y box binding protein 1 (YBX1), promotes germ line stem cell (GSC) maintenance, proliferation, and differentiation in the ovary by preferentially binding to mC-containing RNAs. YPS is genetically demonstrated to function intrinsically for GSC maintenance, proliferation, and progeny differentiation in the ovary, and human YBX1 can functionally replace YPS to support normal GSC development. Highly conserved cold-shock domains (CSDs) of YPS and YBX1 preferentially bind to mC RNA in vitro. Moreover, YPS also preferentially binds to mC-containing RNAs, including mRNAs, in germ cells. The crystal structure of the YBX1 CSD-RNA complex reveals that both hydrophobic stacking and hydrogen bonds are critical for mC binding. Overexpression of RNA-binding-defective YPS and YBX1 proteins disrupts GSC development. Taken together, our findings show that mC RNA modification plays an important role in adult stem cell development.
PubMed: 32015133
DOI: 10.1073/pnas.1910862117
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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건을2024-11-06부터공개중

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