Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Defective translocation of a signal sequence mutant in a prlA4 suppressor strain of Escherichia coli.

European journal of biochemistry - 1 Nov 2002

Adams Hendrik, Scotti Pier A, Luirink Joen, Tommassen Jan

Abstract excerpt

In the accompanying paper [Adams, H., Scotti, P.A., de Cock, H., Luirink, J. & Tommassen, J. (2002) Eur. J. Biochem.269, 5564-5571], we showed that the precursor of outer-membrane protein PhoE of Escherichia coli with a Gly to Leu substitution at position -10 in the signal sequence (G-10L) is targeted to the SecYEG translocon via the signal-recognition particle (SRP) route, instead of via the SecB pathway. Here,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cross-Linking Reagents
Share to Endopeptidase K
Share to Glycine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Intracellular Membranes

Share to Leucine

Share to Protein Biosynthesis

Share to Protein Transport

Share to SEC Translocation Channels

Source

Identifiers

PMID: 12423356
DOI: 10.1046/j.1432-1033.2002.03263.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Defective translocation of a signal sequence mutant in a prlA4 suppressor strain of Escherichia coli.PMID 12423356Read ↗

The F286Y mutation of PrlA4 tempers the signal sequence suppressor phenotype by reducing the SecA binding affinity.Semantic proximity Read ↗

The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.Semantic proximity Read ↗

PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains.Semantic proximity Read ↗

Novel prlA alleles defective in supporting staphylokinase processing in Escherichia coli.Semantic proximity Read ↗

prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli.Semantic proximity Read ↗

The presence of a helix breaker in the hydrophobic core of signal sequences of secretory proteins prevents recognition by the signal-recognition particle in Escherichia coli.Semantic proximity Read ↗

Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein.Semantic proximity Read ↗

Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase.Semantic proximity Read ↗

A signal sequence is not required for protein export in prlA mutants of Escherichia coli.Semantic proximity Read ↗

Structure, function, and biogenesis of SecY, an integral membrane protein involved in protein export.Semantic proximity Read ↗

Modeling the effects of prl mutations on the Escherichia coli SecY complex.Semantic proximity Read ↗

Characterization of cold-sensitive secY mutants of Escherichia coli.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.