Evidence map›Paper›PMID 19293157›Full record

ArticleThe Journal of biological chemistry2009

The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity.

Naomi J Marty, Dakshinamurthy Rajalingam, Alicia D Kight, Nathaniel E Lewis, Daniel Fologea, Thallapuranam Krishnaswamy Suresh Kumar, Ralph L Henry, Robyn L Goforth

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 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
1.5field-weighted citation impact, top 19% 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, 26 citations in OpenAlex.

  1. Article
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  9. ALB3 Insertase Mediates Cytochrome bScientific reports · 2016
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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

8 authors at 1 institution in 1 country.

Naomi J MartyDepartment of Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701, USA.
Dakshinamurthy Rajalingam
Alicia D Kight
Nathaniel E Lewis
Daniel Fologea
Thallapuranam Krishnaswamy Suresh Kumar
Ralph L Henry
Robyn L Goforth
University of Arkansas at Fayetteville · US

Funding

Structure based drug discoveryP20RR015569 · NCRR · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2000 to 2009
$21.4M
NCRR NIH HHS P20RR15569
6 · The paper itself

Abstract

The chloroplast signal recognition particle (cpSRP) and its receptor (cpFtsY) function in thylakoid biogenesis to target integral membrane proteins to thylakoids. Unlike cytosolic SRP receptors in eukaryotes, cpFtsY partitions between thylakoid membranes and the soluble stroma. Based on sequence alignments, a membrane-binding motif identified in Escherichia coli FtsY appears to be conserved in cpFtsY, yet whether the proposed motif is responsible for the membrane-binding function of cpFtsY has yet to be shown experimentally. Our studies show that a small N-terminal region in cpFtsY stabilizes a membrane interaction critical to cpFtsY function in cpSRP-dependent protein targeting. This membrane-binding motif is both necessary and sufficient to direct cpFtsY and fused passenger proteins to thylakoids. Our results demonstrate that the cpFtsY membrane-binding motif may be functionally replaced by the corresponding region from E. coli, confirming that the membrane-binding motif is conserved among organellar and prokaryotic homologs. Furthermore, the capacity of cpFtsY for lipid binding correlates with liposome-induced GTP hydrolysis stimulation. Mutations that debilitate the membrane-binding motif in cpFtsY result in higher rates of GTP hydrolysis, suggesting that negative regulation is provided by the intact membrane-binding region in the absence of a bilayer. Furthermore, NMR and CD structural studies of the N-terminal region and the analogous region in the E. coli SRP receptor revealed a conformational change in secondary structure that takes place upon lipid binding. These studies suggest that the cpFtsY membrane-binding motif plays a critical role in the intramolecular communication that regulates cpSRP receptor functions at the membrane.

Indexed as

AlanineAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionArabidopsisArabidopsis ProteinsBacterial ProteinsChloroplast ProteinsChloroplastsCircular DichroismEscherichia coliGTP PhosphohydrolasesHydrolysisIntracellular MembranesLight-Harvesting Protein ComplexesLipid BilayersAlanineArabidopsis ProteinsBacterial ProteinsChloroplast ProteinscpFtsY protein, ArabidopsisFtsY protein, BacteriaGTP PhosphohydrolasesLight-Harvesting Protein ComplexesLipid BilayersLiposomesMembrane ProteinsNucleotidesPeptidesPhenylalanineReceptors, Cytoplasmic and Nuclear

Identifiers

PMID19293157
PMCPMC2685671
OpenAlexW2010048393

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.