Diversity in the serine recombinases

Margaret Caroline MacHin Smith, H. M. Thorpe

Research output: Contribution to journalArticle

219 Citations (Scopus)

Abstract

Most site-specific recombinases fall into one of two families, based on evolutionary and mechanistic relatedness. These are the tyrosine recombinases or lambda integrase family and the serine recombinases or resolvase/invertase family. The tyrosine recombinases are structurally diverse and functionally versatile and include integrases, resolvases, invertases and transposases. Recent studies have revealed that the serine recombinase family is equally versatile and members have a variety of structural forms. The archetypal resolvase/invertases are highly regulated, only affect resolution or inversion and they have an N-terminal catalytic domain and a C-terminal DNA binding domain. Phage-encoded serine recombinases (e.g. phi C31 integrase) cause integration and excision with strictly controlled directionality, and have an N-terminal catalytic domain but much longer C-terminal domains compared with the resolvase/invertases. This high molecular weight group also contains transposases (e.g. TnpX from Tn4451 ). Other transposases, which belong to a third structurally different group, are similar in size to the resolvase/invertases but have the DNA binding domain N-terminal to the catalytic domain (e.g. IS607 transposase). These three structural groups represented by the resolvase/invertases, the large serine recombinases and relatives of IS607 transposase correlate with three major groupings seen in a phylogeny of the catalytic domains. These observations indicate that the serine recombinases are modular and that fusion of the catalytic domain to unrelated sequences has generated structural and functional diversity.

Original languageEnglish
Pages (from-to)299-307
Number of pages8
JournalMolecular Microbiology
Volume44
DOIs
Publication statusPublished - 2002

Keywords

  • SITE-SPECIFIC RECOMBINATION
  • CONJUGATIVE TRANSPOSON TN5397
  • CLOSTRIDIUM-PERFRINGENS
  • MAMMALIAN-CELLS
  • STRAND EXCHANGE
  • LARGE RESOLVASE
  • TN3 RESOLVASE
  • CRYSTAL-STRUCTURE
  • PHAGE INTEGRASE
  • DNA INVERSION

Cite this

Diversity in the serine recombinases. / Smith, Margaret Caroline MacHin; Thorpe, H. M.

In: Molecular Microbiology, Vol. 44, 2002, p. 299-307.

Research output: Contribution to journalArticle

Smith, Margaret Caroline MacHin ; Thorpe, H. M. / Diversity in the serine recombinases. In: Molecular Microbiology. 2002 ; Vol. 44. pp. 299-307.
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