Literature summary for 3.1.26.13 extracted from

Boso, G.; Oervell, C.; Somia, N.
The nature of the N-terminal amino acid residue of HIV-1 RNase H is critical for the stability of reverse transcriptase in viral particles (2015), J. Virol., 89, 1286-1297 .

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Protein Variants

Protein Variants	Comment	Organism
additional information	mutation of the N-terminal residue of RNase H which is important in the life cycle of HIV-1, change of this residue to several different amino acids. Selection of mutants is based on the N-end rule designation or the structure of the specific amino acid compared to that of the wild-type residue of tyrosine. Compared to wild-type AETF/YVD, the mutants show the following cleavage sites: AETF/MVD, AETF/FVD, AETF/WVD, AETF/TVD, AETF/LVD, AETF/KVD, AETF/AVD, AETF/PVD, AETF/GVD, AETF/SVD, and AETF/VVD, being stabilizing or destabilizing for the N-end rule, packaging and processing of viral polyproteins with RNaseH N-terminal mutations, overview. Reverse transcriptase with an RNase H N-terminal mutation is still degraded in the absence of active viral protease	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	HIV-1	-

Synonyms

Synonyms	Comment	Organism
HIV-1 RNase H	-	Human immunodeficiency virus 1

General Information

General Information	Comment	Organism
evolution	the N-terminal amino acid residue of HIV-1 RNase H is highly conserved	Human immunodeficiency virus 1
malfunction	RNase H N-terminal mutations impact intravirion protein levels and viral infectivity. Reverse transcriptase (RT) with an RNaseHN-terminal mutation is still degraded in the absence of active viral protease	Human immunodeficiency virus 1
physiological function	the nature of the N-terminal amino acid residue of HIV-1 RNase H is critical for the stability of reverse transcriptase (RT) in viral particles. Degradation of reverse transcriptase (RT) in RNase H N-terminal mutants occurs in the absence of active viral protease in the virion. Importance of the RNase H N-terminal residue in the dimerization of RT subunits. RNase H is an HIV-1 protein that has the potential to be a substrate for the N-end rule pathway, which is an ubiquitin-dependent proteolytic system in which the identity of the N-terminal amino acid determines the half-life of a protein. HIV-1 proteins are initially made as part of a polyprotein that is cleaved by the viral protease into the proteins that form the virus particle, RT is subject to an internal cleavage event leading to the formation of two subunits in the virion: a p66 subunit and a p51 subunit that lacks the RNase H domain. Importance of the N-terminal amino acid residue of RNase H in the early life cycle of HIV-1	Human immunodeficiency virus 1

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Release 2023.1 (January 2023)