Evidence map›Paper›PMID 16618969›Full record

ArticleRNA (New York, N.Y.)2006

Residues in two homology blocks on the amino side of the tRNase Z His domain contribute unexpectedly to pre-tRNA 3' end processing.

Neela Zareen, Angela Hopkinson, Louis Levinger

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Neela ZareenYork College of The City University of New York, Jamaica, 11451, USA.
Angela Hopkinson
Louis Levinger
York College, City University of New York · US

Funding

UNIQUELY LABELED AMINO ACIDS FOR PROTEIN NMRS06GM008153 · NIGMS · YORK COLLEGE · PI JOHNSON, LAWRENCE WILLIAM · 1989 to 2008
$13.8M
NIGMS NIH HHS S06 GM008153NIGMS NIH HHS S06GM08153
6 · The paper itself

Abstract

tRNase Z, which can endonucleolytically remove pre-tRNA 3'-end trailers, possesses the signature His domain (HxHxDH; Motif II) of the beta-lactamase family of metal-dependent hydrolases. Motif II combines with Motifs III-V on its carboxy side to coordinate two divalent metal ions, constituting the catalytic core. The PxKxRN loop and Motif I on the amino side of Motif II have been suggested to modulate tRNase Z activity, including the anti-determinant effect of CCA in mature tRNA. Ala walks through these two homology blocks reveal residues in which the substitutions unexpectedly reduce catalytic efficiency. While substitutions in Motif II can drastically affect k(cat) without affecting k(M), five- to 15-fold increases in k(M) are observed with substitutions in several conserved residues in the PxKxRN loop and Motif I. These increases in k(M) suggest a model for substrate binding. Expressed tRNase Z processes mature tRNA with CCA at the 3' end approximately 80 times less efficiently than a pre-tRNA possessing natural sequence of the 3'-end trailer, due to reduced k(cat) with no effect on k(M), showing the CCA anti-determinant to be a characteristic of this enzyme.

Indexed as

RNA Processing, Post-TranscriptionalAlanineAmino Acid MotifsAmino Acid SequenceAnimalsArginineBacillus subtilisbeta-LactamasesDrosophila ProteinsEndoribonucleasesGlycineHistidineMolecular Sequence DataPoint MutationProtein Structure, SecondaryProtein Structure, TertiaryAlanineArgininebeta-LactamasesDrosophila ProteinsEndoribonucleasesGlycineHistidineRNA PrecursorsRNA, TransfertRNase Z, Drosophila

Identifiers

PMID16618969
PMCPMC1464858
OpenAlexW2150425483

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.