Subdomain organization and catalytic residues of the F factor TraI relaxase domain-Reference-Cited by-同舟云学术

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Subdomain organization and catalytic residues of the F factor TraI relaxase domain

Published:2003-03 Issue:1-2 Volume:1646 Page:86-99
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Street Lara M.,Harley Matthew J.,Stern Jennifer C.,Larkin Chris,Williams Sarah L.,Miller Dana L.,Dohm Julie A.,Rodgers Michael E.,Schildbach Joel F.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference48 articles.

1. The Horizontal Gene Pool;Zechner,2000

2. Two active-site tyrosyl residues of protein TrwC act sequentially at the origin of transfer during plasmid R388 conjugation

3. Nicking by transesterification: the reaction catalysed by a relaxase

4. Relaxase (TraI) of IncP alpha plasmid RP4 catalyzes a site-specific cleaving-joining reaction of single-stranded DNA.

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2. Exploration and Application of DNA-Binding Proteins to Make a Versatile DNA–Protein Covalent-Linking Patch (D-Pclip): The Case of a Biosensing Element;Journal of the American Chemical Society;2024-01-31

3. ggMOB: Elucidation of genomic conjugative features and associated cargo genes across bacterial genera using genus-genus mobilization networks;Frontiers in Genetics;2022-12-08

4. Integrative and Conjugative Elements (ICE) and Associated Cargo Genes within and across Hundreds of Bacterial Genera;2020-04-09

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