Studies on the host cell factor functioning in the folding and capsid assembly of gag polyprotein of M-PMV = M-PMV Gag 중합단백질의 구조, 캡시드 형성에 작용하는 숙주세포 인자에 관한 연구

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The carboxy-terminus of the gag gene of Mason-Pfizer monkey virus (M-PMV), the prototype immunosuppressive primate type D retrovirus, encodes a 36-amino acid, proline-rich protein domain that, in the mature virion, becomes the p4 capsid protein. The p4 domain has no known role in M-PMV replication. We found that two mutants with premature termination codons that remove half or all of the p4 domain produced lower levels of stable Gag protein and of self-assembled capsids. Interestingly, yeast two-hybrid screening revealed that p4 specifically interacted with TCP-1γ, a subunit of the chaperonin TRiC (TCP-1 ring complex). TRiC is a cytosolic chaperonin that is known to be involved in both folding and subunit assembly of a variety of cellular proteins. TCP-1γ also associated with high specificity with p6, a similar proline-rich domain of human immunodeficiency virus type 1 (HIV-1). Moreover, in cells, Gag polyprotein associated with the TRiC chaperonin complex and this association depended on ATP hydrolysis. In the p4 truncation mutants, the Gag-TRiC association was greatly reduced. These results strongly suggest that the cytosolic chaperonin TRiC is involved in Gag folding and/or capsid assembly. We propose that TRiC associates transiently with nascent M-PMV Gag molecules to assist in their folding. Consequently, properly folded Gag molecules carry out the intermolecular interactions involved in self-assembly of the immature capsid.
Chung, An-Sik정안식
한국과학기술원 : 생물과학과,
Issue Date
165633/325007 / 000975426

학위논문(박사) - 한국과학기술원 : 생물과학과, 2001.2, [ x, 112 p. ]


리트로 바이러스; 샤페론; Chaperonin; 구조; Folding; Assembly

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