Unknown,Transcriptomics,Genomics,Proteomics

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Accumulation of noncoding RNA due to an RNase P defect in Saccharomyces cerevisiae


ABSTRACT: To investigate the possible range of additional RNase P substrates in vivo a strand-specific, high-density microarray was used to analyze what RNA accumulates with a mutation in the catalytic RNA subunit of nuclear RNase P in Saccharomyces cerevisiae. A wide variety of noncoding RNAs were shown to accumulate, suggesting nuclear RNase P participates in the turnover of normally unstable nuclear RNAs. In some cases, the accumulated noncoding RNAs were shown to be antisense to transcripts that commensurately decreased in abundance. Pre-mRNAs containing introns also accumulated broadly, consistent with either compromised splicing or failure to efficiently turnover pre-mRNAs that do not enter the splicing pathway. Taken together with the high complexity of the nuclear RNase P holoenzyme and its relatively non-specific capacity to bind and cleave mixed sequence RNAs, these data suggest nuclear RNase P facilitates turnover of nuclear RNAs in addition to its role in pre-tRNA biogenesis.

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: Michael Marvin 

PROVIDER: E-MEXP-3140 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

Accumulation of noncoding RNA due to an RNase P defect in Saccharomyces cerevisiae.

Marvin Michael C MC   Clauder-Münster Sandra S   Walker Scott C SC   Sarkeshik Ali A   Yates John R JR   Steinmetz Lars M LM   Engelke David R DR  

RNA (New York, N.Y.) 20110610 8


Ribonuclease P (RNase P) is an essential endoribonuclease that catalyzes the cleavage of the 5' leader of pre-tRNAs. In addition, a growing number of non-tRNA substrates have been identified in various organisms. RNase P varies in composition, as bacterial RNase P contains a catalytic RNA core and one protein subunit, while eukaryotic nuclear RNase P retains the catalytic RNA but has at least nine protein subunits. The additional eukaryotic protein subunits most likely provide additional functio  ...[more]

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