Evidence map›Paper›PMID 19095620›Full record

ArticleRNA (New York, N.Y.)2009

Pre-tRNA turnover catalyzed by the yeast nuclear RNase P holoenzyme is limited by product release.

John Hsieh, Scott C Walker, Carol A Fierke, David R Engelke

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 32 citations in OpenAlex.

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  17. Broadening the mission of an RNA enzyme.Journal of cellular biochemistry · 2009
    Review
  18. Article
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

John HsiehDepartment of Chemistry, University of Michigan, Ann Arbor, 48109-0606, USA.
Scott C Walker
Carol A Fierke
David R Engelke
University of Michigan · US

Funding

ENZYMOLOGY OF RNA PROCESSING ENZYMESR01GM055387 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FIERKE, CAROL A · 1997 to 2014
$4.3M
EUKARYOTIC TRNA MATURATIONR01GM034869 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ENGELKE, DAVID R · 1985 to 2006
$2.3M
NIGMS NIH HHS GM34869NIGMS NIH HHS GM55387NIGMS NIH HHS R01 GM034869NIGMS NIH HHS R01 GM055387
6 · The paper itself

Abstract

Ribonuclease P (RNase P) is a ribonucleoprotein that catalyzes the 5' maturation of precursor transfer RNA in the presence of magnesium ions. The bacterial RNase P holoenzyme consists of one catalytically active RNA component and a single essential but catalytically inactive protein. In contrast, yeast nuclear RNase P is more complex with one RNA subunit and nine protein subunits. We have devised an affinity purification protocol to gently and rapidly purify intact yeast nuclear RNase P holoenzyme for transient kinetic studies. In pre-steady-state kinetic studies under saturating substrate concentrations, we observed an initial burst of tRNA formation followed by a slower, linear, steady-state turnover, with the burst amplitude equal to the concentration of the holoenzyme used in the reaction. These data indicate that the rate-limiting step in turnover occurs after pre-tRNA cleavage, such as mature tRNA release. Additionally, the steady-state rate constants demonstrate a large dependence on temperature that results in nonlinear Arrhenius plots, suggesting that a kinetically important conformational change occurs during catalysis. Finally, deletion of the 3' trailer in pre-tRNA has little or no effect on the steady-state kinetic rate constants. These data suggest that, despite marked differences in subunit composition, the minimal kinetic mechanism for cleavage of pre-tRNA catalyzed by yeast nuclear RNase P holoenzyme is similar to that of the bacterial RNase P holoenzyme.

Indexed as

CatalysisHoloenzymesKineticsNucleic Acid ConformationRibonuclease PRNA PrecursorsSaccharomyces cerevisiae ProteinsSubstrate SpecificityHoloenzymesRibonuclease PRNA PrecursorsSaccharomyces cerevisiae Proteins

Identifiers

PMID19095620
PMCPMC2648709
OpenAlexW2099088591

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.