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Article

Increased protein flexibility leads to promiscuous protein--DNA interactions in type IC restriction-modification systems.

The EMBO journal - 1 Apr 1991

Gubler M, Bickle T A

Abstract excerpt

We have investigated the role of a four amino acid element that is repeated twice and three times, respectively, in the specificity polypeptides of the two allelic restriction-modification systems EcoR124 and EcoR124/3. We had earlier shown that this difference in amino acid sequence between the two systems is solely responsible for the different DNA sequence specificities of the two systems. The effect of single...

Topics

Alleles
Amino Acid Sequence
Bacteriophage lambda
Base Sequence
Binding Sites
DNA
DNA Modification Methylases
DNA Restriction Enzymes
Deoxyribonuclease EcoRI
Escherichia coli
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Plasmids

Protein Binding

Restriction Mapping

Substrate Specificity

Source

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Identifiers

PMID: 1849078
DOI: 10.1002/j.1460-2075.1991.tb08029.x
PMCID: PMC452739

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1849078-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Increased protein flexibility leads to promiscuous protein--DNA interactions in type IC restriction-modification systems.PMID 1849078Read ↗

Structural insights into assembly, operation and inhibition of a type I restriction-modification system.Semantic proximity Read ↗

Characterization of an EcoR124I restriction-modification enzyme produced from a deleted form of the DNA-binding subunit, which results in a novel DNA specificity.Semantic proximity Read ↗

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