Substrate recognition by retroviral integrases
- PMID: 10384243
- DOI: 10.1016/s0065-3527(08)60307-3
Substrate recognition by retroviral integrases
Abstract
Substrate recognition by the retroviral IN enzyme is critical for retroviral integration. To catalyze this recombination event, IN must recognize and act on two types of substrates, viral DNA and host DNA, yet the necessary interactions exhibit markedly different degrees of specificity. Although particular sequences at the viral DNA termini are recognized by IN, many host DNA sequences can serve as the target for integration. Over the last decade, both in vitro and in vivo data have contributed to our understanding of how IN recognizes its substrates. This review provides an overview of the sequence and structure requirements for recognition of viral and host DNA by different retroviral INs and discusses recent progress in mapping protein domains involved in these interactions.
Similar articles
-
Nucleophile selection for the endonuclease activities of human, ovine, and avian retroviral integrases.J Biol Chem. 2001 Jan 5;276(1):114-24. doi: 10.1074/jbc.M007032200. J Biol Chem. 2001. PMID: 11024025
-
Major and minor groove contacts in retroviral integrase-LTR interactions.Biochemistry. 1999 Mar 23;38(12):3624-32. doi: 10.1021/bi982124i. Biochemistry. 1999. PMID: 10090749
-
Structure and function of retroviral integrase.Nat Rev Microbiol. 2022 Jan;20(1):20-34. doi: 10.1038/s41579-021-00586-9. Epub 2021 Jul 9. Nat Rev Microbiol. 2022. PMID: 34244677 Free PMC article. Review.
-
Retroviral intasome assembly and inhibition of DNA strand transfer.Nature. 2010 Mar 11;464(7286):232-6. doi: 10.1038/nature08784. Epub 2010 Jan 31. Nature. 2010. PMID: 20118915 Free PMC article.
-
Retroviral Integrase Structure and DNA Recombination Mechanism.Microbiol Spectr. 2014 Dec;2(6). doi: 10.1128/microbiolspec.MDNA3-0024-2014. Microbiol Spectr. 2014. PMID: 26104441 Review.
Cited by
-
Investigation of formation, recognition, stabilization, and conversion of dimeric G-quadruplexes of HIV-1 integrase inhibitors by electrospray ionization mass spectrometry.J Am Soc Mass Spectrom. 2008 Apr;19(4):550-9. doi: 10.1016/j.jasms.2008.01.012. Epub 2008 Feb 5. J Am Soc Mass Spectrom. 2008. PMID: 18313939
-
Quantitative analysis of HIV-1 preintegration complexes.Methods. 2009 Apr;47(4):283-90. doi: 10.1016/j.ymeth.2009.02.005. Epub 2009 Feb 20. Methods. 2009. PMID: 19233280 Free PMC article.
-
A substitution in rous sarcoma virus integrase that separates its two biologically relevant enzymatic activities.J Virol. 2005 Apr;79(8):4691-9. doi: 10.1128/JVI.79.8.4691-4699.2005. J Virol. 2005. PMID: 15795255 Free PMC article.
-
Pre-organized structure of viral DNA at the binding-processing site of HIV-1 integrase.Nucleic Acids Res. 2005 Apr 6;33(6):1970-81. doi: 10.1093/nar/gki346. Print 2005. Nucleic Acids Res. 2005. PMID: 15814814 Free PMC article.
-
An amino acid in the central catalytic domain of three retroviral integrases that affects target site selection in nonviral DNA.J Virol. 2003 Mar;77(6):3838-45. doi: 10.1128/jvi.77.6.3838-3845.2003. J Virol. 2003. PMID: 12610159 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Other Literature Sources