Source:http://linkedlifedata.com/resource/pubmed/id/15081402
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
2004-4-14
|
pubmed:abstractText |
LRP130 (also known as a LRPPRC) is an RNA and single-stranded DNA-binding protein, and recently identified as a candidate gene responsible for the Leigh syndrome, a French-Canadian type cytochrome c oxidase deficiency. However, the biological function of LRP130 still remains largely unresolved. In the present study, we found that the C-terminal half of the mouse LRP130 located within a 120 amino acid sequence (a.a. 845-964) binds to synthetic RNA homopolymers, poly(G), poly(U), and poly(C), as well as r(CUGCC)(6). Assessment of the subcellular localization indicated both nuclear/endoplasmic reticulum (ER) and mitochondrial fractions to be positive. To further analyze the subcellular localization of LRP130, a nuclear/ER fraction was fractionated into the nucleoplasm (NP) and nuclear envelope (NE)/ER, and the latter was further separated into outer nuclear membrane (ONM)/ER and inner nuclear membrane (INM) by treatment with Triton X-100. LRP130 was detectable in all three fractions, and the distribution pattern was in good accordance with that known for ONM/ER proteins. Interestingly, immunostaining of HeLa cells demonstrated nuclear rim staining of LRP130, specifically at the outside of the NE and also at ER, and association of LRP130 with poly(A)(+) RNA was restricted only to the ONM/ER fraction. Overexpression of full-length mouse LRP130 fused with EGFP resulted in nuclear accumulation of poly(A)(+) RNA in HeLa cells. Taking all these results together, it is suggested that LRP130, a novel type of RNA-binding protein, associates with mRNA/mRNP complexes at the outside of NE and ER, and plays a role in control of mRNA metabolisms.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/LRPPRC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lrpprc protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
7
|
pubmed:volume |
317
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
736-43
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:15081402-Animals,
pubmed-meshheading:15081402-Cell Nucleus,
pubmed-meshheading:15081402-Endoplasmic Reticulum,
pubmed-meshheading:15081402-HeLa Cells,
pubmed-meshheading:15081402-Humans,
pubmed-meshheading:15081402-Intracellular Membranes,
pubmed-meshheading:15081402-Mice,
pubmed-meshheading:15081402-Microscopy, Fluorescence,
pubmed-meshheading:15081402-Neoplasm Proteins,
pubmed-meshheading:15081402-RNA, Messenger,
pubmed-meshheading:15081402-RNA-Binding Proteins,
pubmed-meshheading:15081402-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:15081402-Subcellular Fractions
|
pubmed:year |
2004
|
pubmed:articleTitle |
LRP130, a single-stranded DNA/RNA-binding protein, localizes at the outer nuclear and endoplasmic reticulum membrane, and interacts with mRNA in vivo.
|
pubmed:affiliation |
Biochemistry Division, National Cancer Center Research Institute, 5-1-1 Tsukiji Chuo-ku, Tokyo 104-0045, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|