A relationship between plasmid structure, structural lability, and sensitivity to site-specific endonucleases in Neisseria gonorrhoeae

1 January 1980

journal article
research article
Published by Springer Nature in Molecular Genetics and Genomics

Vol. 177 (2) , 251-260
https://doi.org/10.1007/bf00267436

Abstract

Nearly all gonococcal strains carry a small “phenotypically cryptic” plasmid of approximately 4,200 basepairs. A detailed physical map of this plasmid has been constructed, revealing the presence of numerous putative inverted repeats. These studies also revealed the presence on the plasmid of recognition sequences for several site-specific endonucleases (particularly HpaII, MspI and AluI) that are particularly resistant to cleavage, and confirmed previous reports of structural lability. Both the sites that are resistant to cleavage, and the observed structural variation are associated with the inverted repetitive sequences.

Keywords

This publication has 26 references indexed in Scilit:

Nucleotide sequence of the transposable DNA-element IS2
Nucleic Acids Research, 1979
Direct detection of methylated cytosine in DNA by use of the restriction enzyme Mspl
Nucleic Acids Research, 1979
DNA sequence of the transposable element IS1
Molecular Genetics and Genomics, 1979
Isolation and characterization of DNA repetitions carrying the chromosomal β-lactamase gene of Escherichia coli K-12
Molecular Genetics and Genomics, 1979
pBR322 restriction map derived from the DNA sequence: accurate DNA size markers up to 4361 nucleotide pairs long
Nucleic Acids Research, 1978
Conjugal transfer of R plasmids in Neisseria gonorrhoeae
Nature, 1977
Conjugal Transfer of the Gonococcal Penicillinase Plasmid
Science, 1977
Kinetic studies on the cleavage of adenovirus DNA by restriction endonuclease Eco RI
Nucleic Acids Research, 1976
Nucleotide sequence of region preceding trp mRNA initiation site and its role in promoter and operator function.
Proceedings of the National Academy of Sciences, 1976
Specificity of substrate recognition by the EcoRI restriction endonuclease.
Proceedings of the National Academy of Sciences, 1975