Journal
CELL METABOLISM
Volume 17, Issue 3, Pages 399-410Publisher
CELL PRESS
DOI: 10.1016/j.cmet.2013.02.005
Keywords
-
Categories
Funding
- Swiss National Science Foundation [31003A-141068/1]
- iGE3
- State of Geneva
- BBSRC [BB/F011520/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F011520/1] Funding Source: researchfish
- Medical Research Council [G0700718B] Funding Source: researchfish
- Swiss National Science Foundation (SNF) [31003A_141068] Funding Source: Swiss National Science Foundation (SNF)
Ask authors/readers for more resources
Various specialized domains have been described in the cytosol and the nucleus; however, little is known about compartmentalization within the mitochondrial matrix. GRSF1 (G-rich sequence factor 1) is an RNA binding protein that was previously reported to localize in the cytosol. We found that an isoform of GRSF1 accumulates in discrete foci in the mitochondrial matrix. These foci are composed of nascent mitochondrial RNA and also contain RNase P, an enzyme that participates in mitochondrial RNA processing. GRSF1 was found to interact with RNase P and to be required for processing of both classical and tRNA-less RNA precursors. In its absence, cleavage of primary RNA transcripts is abnormal, leading to decreased expression of mitochondrially encoded proteins and mitochondrial dysfunction. Our findings suggest that the foci containing GRSF1 and RNase P correspond to sites where primary RNA transcripts converge to be processed. We have termed these large ribonucleoprotein structures mitochondrial RNA granules.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available