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Nucleic Acids Research Advance Access originally published online on May 5, 2007
Nucleic Acids Research 2007 35(11):3519-3524; doi:10.1093/nar/gkm071
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Nucleic Acids Research, 2007, Vol. 35, No. 11 3519-3524
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.


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Human RNase P: a tRNA-processing enzyme and transcription factor

Nayef Jarrous* and Robert Reiner

Department of Molecular Biology, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel

*To whom correspondence should be addressed. Tel: 972 2 6758233; Fax: 972 2 6784010; Email: jarrous{at}md.huji.ac.il

Received January 11, 2007. Revised January 24, 2007. Accepted January 24, 2007.

Ribonuclease P (RNase P) has been hitherto well known as a catalytic ribonucleoprotein that processes the 5' leader sequence of precursor tRNA. Recent studies, however, reveal a new role for nuclear forms of RNase P in the transcription of tRNA genes by RNA polymerase (pol) III, thus linking transcription with processing in the regulation of tRNA gene expression. However, RNase P is also essential for the transcription of other small noncoding RNA genes, whose precursor transcripts are not recognized as substrates for this holoenzyme. Accordingly, RNase P can act solely as a transcription factor for pol III, a role that seems to be conserved in eukarya.


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