Evidence map›Paper›PMID 13130133›Full record

ArticleRNA (New York, N.Y.)2003

The extended loops of ribosomal proteins L4 and L22 are not required for ribosome assembly or L4-mediated autogenous control.

Janice M Zengel, Adam Jerauld, Andre Walker, Markus C Wahl, Lasse Lindahl

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

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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

5 authors.

Janice M ZengelDepartment of Biological Sciences, University of Maryland Baltimore County, Baltimore, Maryland 21250, USA. zengel@umbc.edu
Adam Jerauld
Andre Walker
Markus C Wahl
Lasse Lindahl

Funding

PHS HHS 54876
6 · The paper itself

Abstract

Ribosomal proteins L4 and L22 both have a globular domain that sits on the surface of the large ribosomal subunit and an extended loop that penetrates its core. The tips of both loops contribute to the lining of the peptide exit tunnel and have been implicated in a gating mechanism that might regulate the exit of nascent peptides. Also, the extensions of L4 and L22 contact multiple domains of 23S rRNA, suggesting they might facilitate rRNA folding during ribosome assembly. To learn more about the roles of these extensions, we constructed derivatives of both proteins that lack most of their extended loops. Our analysis of ribosomes carrying L4 or L22 deletion proteins did not detect any significant difference in their sedimentation property or polysome distribution. Also, the role of L4 in autogenous control was not affected. We conclude that these extensions are not required for ribosome assembly or for L4-mediated autogenous control of the S10 operon.

Indexed as

Escherichia coli ProteinsAmino Acid SequenceBinding SitesEscherichia coliGene DeletionGene Expression Regulation, BacterialModels, MolecularMolecular Sequence DataNucleic Acid ConformationOperonRibosomal ProteinsRibosomesRNA, BacterialRNA-Binding ProteinsRNA, MessengerRNA, Ribosomal, 23SEscherichia coli Proteinsribosomal protein L4Ribosomal ProteinsRNA, BacterialRNA-Binding ProteinsRNA, MessengerRNA, Ribosomal, 23SrplV protein, E coli

Identifiers

PMID13130133
PMCPMC1370483

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.