Literature summary for 3.1.13.2 extracted from

Roda, R.H.; Balakrishnan, M.; Hanson, M.N.; Woehrl, B.M.; Le Grice, S.F.J.; Roques, B.P.; Gorelick, R.J.; Bambara, R.A.
Role of the reverse transcriptase, nucleocapsid protein, and template structure in the two-step transfer mechanism in retroviral recombination (2003), J. Biol. Chem., 278, 31536-31546.

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Organism

Organism	UniProt	Comment	Textmining
equine infectious anemia virus	-	EIAV	-
equine infectious anemia virus EIAV	-	EIAV	-
Human immunodeficiency virus 1	-	HIV-1	-

Purification (Commentary)

Purification (Comment)	Organism
-	Human immunodeficiency virus 1

Reaction

Reaction	Comment	Organism	Reaction ID
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid	The RNase H activity is necessary for strand transfers, which occur through a two-step mechanism. The docking, which is the first step is most efficient when the reverse transcriptase pauses in a way that makes a series of adjacent RNase H cleavages. Invasion at the site is promote at high acceptor concentration and by the presence of nucleocapsid. The locking step is the second, which is most proficient in regions of weak pausing that lack stable structure and is promoted by the chaperone properties of nucleocapsid.	Human immunodeficiency virus 1	a

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Release 2023.1 (January 2023)