TY - JOUR
T1 - Human RNase P ribonucleoprotein is required for formation of initiation complexes of RNA polymerase III
AU - Serruya, Raphael
AU - Orlovetskie, Natalie
AU - Reiner, Robert
AU - Dehtiar-Zilber, Yana
AU - Wesolowski, Donna
AU - Altman, Sidney
AU - Jarrous, Nayef
N1 - Publisher Copyright:
© 2015 The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.
PY - 2015/4/24
Y1 - 2015/4/24
N2 - Human RNase P is implicated in transcription of small non-coding RNA genes by RNA polymerase III (Pol III), but the precise role of this ribonucleoprotein therein remains unknown. We here show that targeted destruction of HeLa nuclear RNase P inhibits transcription of 5S rRNA genes in whole cell extracts, if this precedes the stage of initiation complex formation. Biochemical purification analyses further reveal that this ribonucleoprotein is recruited to 5S rRNA genes as a part of proficient initiation complexes and the activity persists at reinitiation. Knockdown of RNase P abolishes the assembly of initiation complexes by preventing the formation of the initiation sub-complex of Pol III. Our results demonstrate that the structural intactness, but not the endoribonucleolytic activity per se, of RNase P is critical for the function of Pol III in cells and in extracts.
AB - Human RNase P is implicated in transcription of small non-coding RNA genes by RNA polymerase III (Pol III), but the precise role of this ribonucleoprotein therein remains unknown. We here show that targeted destruction of HeLa nuclear RNase P inhibits transcription of 5S rRNA genes in whole cell extracts, if this precedes the stage of initiation complex formation. Biochemical purification analyses further reveal that this ribonucleoprotein is recruited to 5S rRNA genes as a part of proficient initiation complexes and the activity persists at reinitiation. Knockdown of RNase P abolishes the assembly of initiation complexes by preventing the formation of the initiation sub-complex of Pol III. Our results demonstrate that the structural intactness, but not the endoribonucleolytic activity per se, of RNase P is critical for the function of Pol III in cells and in extracts.
UR - http://www.scopus.com/inward/record.url?scp=84936885888&partnerID=8YFLogxK
U2 - 10.1093/nar/gkv447
DO - 10.1093/nar/gkv447
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C2 - 25953854
AN - SCOPUS:84936885888
SN - 0305-1048
VL - 43
SP - 5442
EP - 5450
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 11
ER -
