Leucine zipper domain of HIV-1 gp41 interacted specifically with alpha-catenin.
Interactions between viral and cellular proteins could explain the molecular mechanisms behind the viral life cycle of HIV-1. The envelope protein gp41 of HIV-1 specifically interacted with alpha-catenin, not with beta-catenin. This interaction was shown by in vitro protein assay and in vivo transfected cell systems. Microinjection of the DNA expressing HIV-1 gp160 and alpha-catenin, into the HeLa cell, resulted in the colocalization of gp41 and alpha-catenin. Interestingly the noncleavable mutant of gp160 and alpha-catenin were found to be colocalized in the cell membrane. Mapping of the interaction sites between these two proteins revealed that the leucine zipper-like structure, located between the first and second alpha-helix domains from the carboxy terminus of HIV-1 gp41, interacted strongly with the carboxy terminus of alpha-catenin.
Kim
Jong Tae
JT
Bio-Med RRC, Division of Life Sciences, Pai Chai University, Taejon 302-735, Korea.
Kim
Eun Mi
EM
Lee
Kyoung Hoa
KH
Choi
Ji-Eun
JE
Jhun
Byung H
BH
Kim
Jung Woo
JW
D002462:Cell Membrane / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D015700:HIV Envelope Protein gp41 / Q000737:chemistry / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D016350:Leucine Zippers / Q000502:physiology*; D017434:Protein Structure, Tertiary; D051178:alpha Catenin
C495273:CTNNA1 protein, human; D003598:Cytoskeletal Proteins; D015700:HIV Envelope Protein gp41; D051178:alpha Catenin