Abstract
We have examined the post-translational processing, intrachain disulfide bond formation, folding, and assembly of MHC class I H chains with beta 2-microglobulin after coupled in vitro translation of homogeneous mRNA and transport of nascent chains into canine microsomal vesicles. The formation of native alpha 3 domain conformation was dependent on conditions that optimized intrachain disulfide bond formation, and efficient folding of the alpha 1 alpha 2 domain required exposure to antigenic peptide. beta 2-microglobulin and peptide acted synergistically in forming native alpha 1 alpha 2 domain structure, and a small proportion of molecules with native alpha 1 alpha 2, but non-native alpha 3 structure were detected, indicating that alpha 3 domain folding is not an absolute prerequisite for the formation of native alpha 1 alpha 2 domain structure.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cloning, Molecular
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Drug Synergism
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Electrophoresis, Polyacrylamide Gel
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Gene Products, gag / pharmacology*
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Glutathione / pharmacology
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H-2 Antigens / biosynthesis*
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Histocompatibility Antigen H-2D
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Immediate-Early Proteins*
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In Vitro Techniques
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Mice
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Mice, Inbred BALB C
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Mice, Inbred C57BL
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Microsomes / physiology
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Molecular Conformation
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Molecular Sequence Data
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Protein Biosynthesis / drug effects
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Protein Processing, Post-Translational*
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Transcription, Genetic
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Viral Proteins / pharmacology*
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beta 2-Microglobulin / pharmacology*
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gag Gene Products, Human Immunodeficiency Virus
Substances
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Gene Products, gag
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H-2 Antigens
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Histocompatibility Antigen H-2D
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Immediate-Early Proteins
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Viral Proteins
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beta 2-Microglobulin
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cytomegalovirus immediate early phosphoprotein pp89
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gag Gene Products, Human Immunodeficiency Virus
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p18 gag protein, Human immunodeficiency virus 1
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Glutathione