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Related Experiment Videos

Lambda integrase cleaves DNA in cis

S E Nunes-Düby1, R S Tirumalai, L Dorgai

  • 1Division of Biology and Medicine, Brown University, Providence, RI 02912.

The EMBO Journal
|September 15, 1994
PubMed
Summary
This summary is machine-generated.

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Site-specific recombinases like integrases (Ints) were thought to cleave DNA via a

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Site-specific recombinases (SSRs) are crucial for DNA manipulation.
  • The Int family of SSRs mediates DNA cleavage through a specific tyrosine residue.
  • A 'trans' cleavage model proposes the catalytic tyrosine comes from a separate protein subunit.

Purpose of the Study:

  • To investigate the mechanism of DNA cleavage by Int family recombinases.
  • To determine whether DNA cleavage occurs in 'cis' or 'trans'.

Main Methods:

  • Exploited differences in DNA binding specificity between lambda and HK022 integrases.
  • Utilized bispecific DNA substrates with wild-type and mutant integrases.
  • Analyzed DNA cleavage at individual sites on the substrates.

Related Experiment Videos

Main Results:

  • Analysis of cleavage at individual sites strongly supports 'cis' cleavage.
  • The catalytic tyrosine is provided by the integrase bound to the cleaved DNA site.
  • Contradicts previous findings suggesting 'trans' cleavage for FLP and lambda Int.

Conclusions:

  • Int-family recombinases primarily catalyze DNA cleavage via a 'cis' mechanism.
  • The study reconciles conflicting data on SSR cleavage mechanisms.
  • Suggests Int-family recombinases may possess both 'cis' and 'trans' cleavage capabilities.