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Article

A membrane protein with similarity to N-methylphenylalanine pilins is essential for DNA binding by competent Bacillus subtilis.

Journal of bacteriology - 1 Mar 1990

Breitling R, Dubnau D

Abstract excerpt

In a cloned copy of comG open reading frame 3 (ORF3), an in-frame deletion was generated by site-directed in vitro mutagenesis, removing the coding sequence for 15 amino acids from the central portion of this pilin-related protein. The mutagenized ORF3 was incorporated into the Bacillus subtilis chromosome, replacing the wild-type ORF3. The presence of the deleted ORF3 in the chromosome, as confirmed by Southern...

Topics

Alleles
Amino Acid Sequence
Bacillus subtilis
Bacterial Outer Membrane Proteins
Base Sequence
Chromosome Deletion
Chromosomes, Bacterial
DNA-Binding Proteins
Fimbriae Proteins
Fimbriae, Bacterial
Gene Expression

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Membrane Proteins

Molecular Sequence Data

Mutation

Oligonucleotide Probes

Plasmids

Source

Open in PubMed Open full text

Identifiers

PMID: 1968455
DOI: 10.1128/jb.172.3.1499-1508.1990
PMCID: PMC208626

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1968455-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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A membrane protein with similarity to N-methylphenylalanine pilins is essential for DNA binding by competent Bacillus subtilis.PMID 1968455Read ↗

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