NDLI: Predominant role of amino-terminal sequences in dictating efficiency of class II major histocompatibility complex alpha beta dimer expression.

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Predominant role of amino-terminal sequences in dictating efficiency of class II major histocompatibility complex alpha beta dimer expression.

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Predominant role of amino-terminal sequences in dictating efficiency of class II major histocompatibility complex alpha beta dimer expression.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Braunstein, N. S. Germain, R. N. Sant, A. J.
Description	Author Affiliation: Sant AJ ( Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.);
Abstract	Cell surface expression of class II major histocompatibility complex-encoded (Ia) molecules depends on association of the component alpha and beta chains into a stable heterodimer. In the mouse, two isotypes of class II molecules have been identified, A beta A alpha and E beta E alpha. However, experiments from this laboratory have shown that, following DNA-mediated gene transfer into murine L cells, an A beta E alpha-mixed-isotype molecule can be assembled and expressed at the cell surface. In the present study, we have investigated the structural features of the beta chain that control the extent of association and level of membrane expression of A beta E alpha interisotypic pairs. The use of intact allelic A beta genes demonstrated that only A beta d chains, but not A beta b or A beta k chains, can be coexpressed on the surface membrane with E alpha chains. Transfection of recombinant A beta genes that encode all or half of the beta 1 domain from one allele and the rest of the chain from another allele revealed that the 5-7 polymorphic residues in the amino-terminal 50 residues of the A beta chain completely controlled this variation in expression with E alpha. Isotypically mixed beta genes encoding the A beta 1 domain of either A beta d or A beta k chains and the beta 2, transmembrane, and intracytoplasmic portions of E beta chains were used to assess the role of isotypically conserved structures in alpha beta pairing and expression. In marked contrast to the major alterations in expression accompanying changes in the amino-terminal polymorphic residues, exchange of these carboxyl-terminal isotypic segments had no detectable influence on the efficiency of expression with either A alpha or E alpha chains. These results argue strongly that variations in the efficiency with which distinct Ia alpha beta dimers assemble and are transported to the membrane is determined almost exclusively by a critical chain interaction involving the amino-terminal domains of the molecules.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	84
Language	English
Publisher	National Academy of Sciences
Publisher Date	1987-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Gene Expression Regulation Histocompatibility Antigens Class II Biosynthesis Alleles Animals Biological Transport Genes, MHC Class II Genetics L Cells (Cell Line) Mice Protein Multimerization Protein Processing, Post-Translational Recombinant Fusion Proteins Transfection Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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