Identification of the λ integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation-Reference-Cited by-同舟云学术

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Identification of the λ integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation

Published:2003-06-27 Issue:14 Volume:100 Page:8176-8181
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:PNAS

Author:

Warren David,Sam My D.,Manley Kate,Sarkar Dibyendu,Lee Sang Yeol,Abbani Mohamad,Wojciak Jonathan M.,Clubb Robert T.,Landy Arthur

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference45 articles.

1. The integrase family of recombinases: organization and function of the active site

2. Azaro, M. A. & Landy, A. (2002) in Mobile DNA II, eds. Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A. (Am. Soc. Microbiol., Washington, DC), pp. 118-148.

3. Bacteriophage lambda int protein recognizes two classes of sequence in the phage att site: characterization of arm-type sites.

4. Autonomous DNA binding domains of λ integrase recognize two different sequence families

5. DNA Looping Generated by DNA Bending Protein IHF and the Two Domains of Lambda Integrase

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1. Pandemic Vibrio cholerae shuts down site-specific recombination to retain an interbacterial defence mechanism;Nature Communications;2020-12

2. Cooperative DNA binding by proteins through DNA shape complementarity;Nucleic Acids Research;2019-07-25

3. Pathogenicity Island Cross Talk Mediated by Recombination Directionality Factors Facilitates Excision from the Chromosome;Journal of Bacteriology;2016-03

4. The λ Integrase Site-specific Recombination Pathway;Mobile DNA III;2015-05-26

5. The λ Integrase Site-specific Recombination Pathway;Microbiology Spectrum;2015-04-02

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