Noncovalent SUMO-interaction motifs in HIV integrase play important roles in SUMOylation, cofactor binding, and virus replication

• Published in: Virology journal Vol. 16; no. 1; p. 42
• Main Authors: Zheng, Yingfeng, Jayappa, Kallesh Danappa, Ao, Zhujun, Qiu, Xiangguo, Su, Ruey-Chyi, Yao, Xiaojian
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 02.04.2019; BioMed Central; BMC
• Subjects: Amino Acid Motifs; Amino acid sequence; Amino acids; Analysis; Binding sites; CD4 antigen; Cofactors; Deoxyribonucleic acid; DNA; Enzymes; Epithelium; Event-related potentials; HEK293 Cells; HIV; HIV integrase; HIV Integrase - genetics; HIV Integrase - metabolism; HIV-1 - enzymology; HIV-1 - physiology; Human immunodeficiency virus; Human immunodeficiency virus (HIV); Human immunodeficiency virus 1; Humans; Integrase; Integrase (IN); Integrases; LEDGF/p75; Life cycles; Localization; Lymphocytes T; mutants; mutational analysis; Nuclear transport; physiological transport; Protein Binding; Protein Interaction Domains and Motifs; Protein-protein interaction; Protein-protein interactions; Proteins; Rad52 protein; Real-Time Polymerase Chain Reaction; Replication; Reverse transcription; SUMO protein; SUMO-1 Protein - metabolism; SUMO-interacting motifs (SIMs); SUMOylation; T cells; T-lymphocytes; Ubiquitin; Virus Replication; viruses; Integrase (IN); Nuclear localization; Protein-protein interaction; SUMO-interacting motifs (SIMs); HIV replication; LEDGF/p75; SUMOylation; Human immunodeficiency virus (HIV)

HIV integrase (IN) and its cellular cofactors, including lens-epithelium-derived growth factor (LEDGF/p75), Ku70, p300, and Rad52, are subject to small ubiquitin-like modifier (SUMO) modification. In addition to covalent SUMOylation, SUMO paralogs can also noncovalently bind proteins through SUMO-in...