RRC ID 50418
Author Chou HL, Tian L, Kumamaru T, Hamada S, Okita TW.
Title Multifunctional RNA Binding Protein OsTudor-SN in Storage Protein mRNA Transport and Localization.
Journal Plant Physiol
Abstract The multifunctional RNA-binding protein Tudor-SN plays multiple roles in transcriptional and posttranscriptional processes due to its modular domain structure, consisting of four tandem Staphylococcus nuclease (SN)-like domains (4SN), followed by a carboxyl-terminal Tudor domain, followed by a fifth partial SN sequence (Tsn). In plants, it confers stress tolerance, is a component of stress granules and P-bodies, and may participate in stabilizing and localizing RNAs to specific subdomains of the cortical-endoplasmic reticulum in developing rice (Oryza sativa) endosperm. Here, we show that, in addition to the intact rice OsTudor-SN protein, the 4SN and Tsn modules exist as independent polypeptides, which collectively may coassemble to form a complex population of homodimer and heteroduplex species. The 4SN and Tsn modules exhibit different roles in RNA binding and as a protein scaffold for stress-associated proteins and RNA-binding proteins. Despite their distinct individual properties, mutations in both the 4SN and Tsn modules mislocalize storage protein mRNAs to the cortical endoplasmic reticulum. These results indicate that the two modular peptide regions of OsTudor-SN confer different cellular properties but cooperate in mRNA localization, a process linking its multiple functions in the nucleus and cytoplasm.
Volume 175(4)
Pages 1608-1623
Published 2017-12-1
DOI 10.1104/pp.17.01388
PII pp.17.01388
PMID 29084903
PMC PMC5717745
MeSH Gene Expression Regulation, Plant Models, Molecular Nuclear Proteins / genetics Nuclear Proteins / metabolism* Oryza / metabolism* Plant Proteins / genetics Plant Proteins / metabolism* Protein Conformation Protein Transport RNA, Messenger / genetics RNA, Messenger / metabolism RNA, Plant / metabolism*
IF 6.902
Times Cited 8
Rice Induced mutation lines