Evidence map›Paper›PMID 10430882›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis.

M Sissler, C Delorme, J Bond, S D Ehrlich, P Renault, C Francklyn

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

64 citing papers in PubMed, 136 citations in OpenAlex.

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  9. Comparative genomics of the genusMicrobial genomics · 2020
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4 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

M SisslerDepartment of Biochemistry, College of Medicine, Given Building, University of Vermont, Burlington, VT 05405, USA.
C Delorme
J Bond
S D Ehrlich
P Renault
C Francklyn
University of Vermont · US

Funding

Structure and Mechanism of Class II tRNA SynthetasesR01GM054899 · NIGMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI FRANCKLYN, CHRISTOPHER S · 1997 to 2017
$5.7M
NIGMS NIH HHS GM54899NIGMS NIH HHS R01 GM054899
6 · The paper itself

Abstract

In addition to their essential catalytic role in protein biosynthesis, aminoacyl-tRNA synthetases participate in numerous other functions, including regulation of gene expression and amino acid biosynthesis via transamidation pathways. Herein, we describe a class of aminoacyl-tRNA synthetase-like (HisZ) proteins based on the catalytic core of the contemporary class II histidyl-tRNA synthetase whose members lack aminoacylation activity but are instead essential components of the first enzyme in histidine biosynthesis ATP phosphoribosyltransferase (HisG). Prediction of the function of HisZ in Lactococcus lactis was assisted by comparative genomics, a technique that revealed a link between the presence or the absence of HisZ and a systematic variation in the length of the HisG polypeptide. HisZ is required for histidine prototrophy, and three other lines of evidence support the direct involvement of HisZ in the transferase function. (i) Genetic experiments demonstrate that complementation of an in-frame deletion of HisG from Escherichia coli (which does not possess HisZ) requires both HisG and HisZ from L. lactis. (ii) Coelution of HisG and HisZ during affinity chromatography provides evidence of direct physical interaction. (iii) Both HisG and HisZ are required for catalysis of the ATP phosphoribosyltransferase reaction. This observation of a common protein domain linking amino acid biosynthesis and protein synthesis implies an early connection between the biosynthesis of amino acids and proteins.

Indexed as

Bacterial ProteinsAmino Acid SequenceAmino Acyl-tRNA SynthetasesATP PhosphoribosyltransferaseBacteriaCatalysisEscherichia coliGenetic Complementation TestHistidineKineticsLactococcus lactisMolecular Sequence DataRecombinant ProteinsRNA, Transfer, HisSequence AlignmentSequence Homology, Amino AcidAmino Acyl-tRNA SynthetasesATP PhosphoribosyltransferaseBacterial ProteinsHistidineHisZ protein, Lactococcus lactisRecombinant ProteinsRNA, Transfer, His

Identifiers

PMID10430882
PMCPMC17719
OpenAlexW2111468050

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.