Journal
NUCLEIC ACIDS RESEARCH
Volume 40, Issue 10, Pages 4589-4603Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gks006
Keywords
-
Categories
Funding
- National Institutes of Health [GM57220, GM81554]
Ask authors/readers for more resources
Here we demonstrate a new regulatory mechanism for tRNA processing in Escherichia coli whereby RNase T and RNase PH, the two primary 3' -> 5' exonucleases involved in the final step of 3'-end maturation, compete with poly(A) polymerase I (PAP I) for tRNA precursors in wild-type cells. In the absence of both RNase T and RNase PH, there is a > 30-fold increase of PAP I-dependent poly(A) tails that are 10 nt in length coupled with a 2.3- to 4.2-fold decrease in the level of aminoacylated tRNAs and a > 2-fold decrease in growth rate. Only 7 out of 86 tRNAs are not regulated by this mechanism and are also not substrates for RNase T, RNase PH or PAP I. Surprisingly, neither PNPase nor RNase II has any effect on tRNA poly(A) tail length. Our data suggest that the polyadenylation of tRNAs by PAP I likely proceeds in a distributive fashion unlike what is observed with mRNAs.
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