Structure of Drosophila Oskar reveals a novel RNA binding protein, Proc Natl Acad Sci U S A. 2015 Sep 15; 112(37): 11541–11546.
发布时间：2015年10月16日
PNAS, 2015 Sep 15; 112(37): 11541–11546. Published online 2015 Aug 31. doi: 10.1073/pnas.1515568112
Structure of Drosophila Oskar reveals a novel RNA binding protein
Na Yang,a,b,1,2 Zhenyu Yu,a,1 Menglong Hu,a,1,3 Mingzhu Wang,a Ruth Lehmann,c,d,2 and Rui-Ming Xu a,b,2
Abstract
Oskar (Osk) protein plays critical roles during Drosophila germ cell development, yet its functions in germ-line formation and body patterning remain poorly understood. This situation contrasts sharply with the vast knowledge about the function and mechanism of osk mRNA localization. Osk is predicted to have an N-terminal LOTUS domain (Osk-N), which has been suggested to bind RNA, and a C-terminal hydrolase-like domain (Osk-C) of unknown function. Here, we report the crystal structures of Osk-N and Osk-C. Osk-N shows a homodimer of winged-helix–fold modules, but without detectable RNA-binding activity. Osk-C has a lipase-fold structure but lacks critical catalytic residues at the putative active site. Surprisingly, we found that Osk-C binds the 3′UTRs of osk and nanos mRNA in vitro. Mutational studies identified a region of Osk-C important for mRNA binding. These results suggest possible functions of Osk in the regulation of stability, regulation of translation, and localization of relevant mRNAs through direct interaction with their 3′UTRs, and provide structural insights into a novel protein–RNA interaction motif involving a hydrolase-related domain.
附件下载：
Structure of Drosophila Oskar reveals a novel RNA binding protein, Proc Natl Acad Sci U S A. 2015 Sep 15; 112(37): 11541–11546.
PNAS, 2015 Sep 15; 112(37): 11541–11546. Published online 2015 Aug 31. doi: 10.1073/pnas.1515568112
Structure of Drosophila Oskar reveals a novel RNA binding protein
Na Yang,a,b,1,2 Zhenyu Yu,a,1 Menglong Hu,a,1,3 Mingzhu Wang,a Ruth Lehmann,c,d,2 and Rui-Ming Xu a,b,2
Abstract
Oskar (Osk) protein plays critical roles during Drosophila germ cell development, yet its functions in germ-line formation and body patterning remain poorly understood. This situation contrasts sharply with the vast knowledge about the function and mechanism of osk mRNA localization. Osk is predicted to have an N-terminal LOTUS domain (Osk-N), which has been suggested to bind RNA, and a C-terminal hydrolase-like domain (Osk-C) of unknown function. Here, we report the crystal structures of Osk-N and Osk-C. Osk-N shows a homodimer of winged-helix–fold modules, but without detectable RNA-binding activity. Osk-C has a lipase-fold structure but lacks critical catalytic residues at the putative active site. Surprisingly, we found that Osk-C binds the 3′UTRs of osk and nanos mRNA in vitro. Mutational studies identified a region of Osk-C important for mRNA binding. These results suggest possible functions of Osk in the regulation of stability, regulation of translation, and localization of relevant mRNAs through direct interaction with their 3′UTRs, and provide structural insights into a novel protein–RNA interaction motif involving a hydrolase-related domain.
相关报道：http://www.ibp.cas.cn/kyjz/zxdt/201509/t20150902_4419442.html
文章链接：http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4577175/