TY - JOUR
T1 - Substrate recognition by retroviral integrases.
AU - Katzman, Michael
AU - Katz, R. A.
N1 - Funding Information:
M. K. was supported by W. W. Smith Charitable Trust Research Grants A9601 and A9701 and by Public Health Service Grant AI30759 from the National Institute of Allergy and Infectious Diseases. R. A. K. received support from CA71515, AI40385, AI40721, from institutional Grant CA06927 from the National Institutes of Health, and from an appropriation by the Commonwealth of Pennsylvania. The contents of this manuscript are solely the responsibility of the authors and do not necessarily represent the official views of the National Cancer Institute or any other sponsoring organization.
PY - 1999
Y1 - 1999
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0032608690&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032608690&partnerID=8YFLogxK
U2 - 10.1016/s0065-3527(08)60307-3
DO - 10.1016/s0065-3527(08)60307-3
M3 - Review article
C2 - 10384243
AN - SCOPUS:0032608690
VL - 52
SP - 371
EP - 395
JO - Advances in Virus Research
JF - Advances in Virus Research
SN - 0065-3527
ER -