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Tamarin: Principles of Genetics, Seventh Edition
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III. Molecular Genetics
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16. Gene Expression: Control in Eukaryotes
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NH2 V
C Membrane
COOH
Figure 16.43 The T-cell receptor is made up of two protein chains, and , anchored in the cell membrane. Each protein is similar to an immunoglobulin chain and is created the same way, with V-J types of joining taking place. (a) The gene complex is composed of numerous V and J genes and one constant gene. The gene complex has V, D, J, and C genes. (b) Each protein chain has two domains, similar to the domains of the immunoglobulins, indicating a common evolutionary ancestry.
groove is bound on both sides so that the presented polypeptide is small and defined (fig. 16.45). In the class II protein, the groove is unbound, allowing for a longer polypeptide ( g. 16.46). Class I MHC proteins are found on almost all cells. The polypeptides that an infected cell presents with the MHC I proteins come from the breakdown of proteins within the cytoplasm of the cell. Peptides are targeted for breakdown when a ubiquitin molecule binds to the protein, sending a cellular signal that the protein is to be degraded. (Ubiquitin is a small polypeptide of 76 amino acid residues, highly conserved in eukaryotes.) The ubiquitintagged protein is unfolded, in an ATP-dependent process, and then fed into a proteasome, a barrel-shaped cellular organelle for protein breakdown ( g. 16.47). Then the peptide fragments associate with two proteins, together called TAP (transporter for antigen processing), that prevent further degradation of the peptide as well as transport the peptide into the endoplasmic reticulum, where the peptide binds to the class I MHC proteins. The MHC I proteins with antigen are then transported to the cell surface. Passing T cells, called killer T cells or CD8 T cells because of their CD8 receptor protein, recognize the foreign antigen presented by the MHC I protein and release substances that kill the infected cells ( g. 16.48a ). ( White blood cells are classi ed by their surface antigens; the CD designation comes from cluster of differentiation antigens used for this purpose.)
Figure 16.44 The major histocompatibility complex (MHC) class I protein (a) is composed of two protein chains. The chain is composed of three domains similar to the immunoglobulins and T-cell receptors. The second chain is 2 macroglobulin. The MHC class II protein (b) is composed of an and a chain. The MHC proteins present antigens to the T-cell receptors to signal that a foreign agent has invaded the cell.
Tamarin: Principles of Genetics, Seventh Edition
III. Molecular Genetics
16. Gene Expression: Control in Eukaryotes
The McGraw Hill Companies, 2001
Sixteen
Gene Expression: Control in Eukaryotes
A three-dimensional computer model of the antigen-presenting site of an MHC class I protein. The presented peptide is nine amino acid residues long and internally bound at each end. (Courtesy of Don C. Wiley.)
Class II MHC proteins are found only on cells involved in the immune system, such as macrophages and B lymphocytes. These cells are most likely to have encountered foreign objects like bacteria or parasites by having engulfed them. The MHC II proteins present foreign antigens not from the cytoplasm, but from endo-
somic vesicles within the cells. These vesicles form by budding from the cell surface and often contain foreign proteins and protease enzymes. The MHC II proteins migrate into the vesicles, where they pick up foreign polypeptides and then migrate to the cell surface. The response of passing T cells to the presentation by MHC II proteins is different from the response to MHC I proteins. The MHC II proteins with antigens are recognized by helper T cells, also called CD4 cells because of their surface receptor protein. Rather than kill cells such as infected macrophages that are useful in the immune system, the helper T cells stimulate the macrophages to destroy the foreign bacteria in their endosomic vesicles. The helper T cells also activate antibody-producing B cells. CD4 cells are the prime targets of the HIV virus, making individuals with AIDS very prone to bacterial infections and other immune problems (box 16.3). One last point is worth mentioning about the MHC system.The loci for MHC proteins do not have V(D)J joining to produce the high levels of variability found in B and T cells. The MHC loci are, however, very variable, with many alleles. (That variability is one reason why organ transplants are usually rejected without immunosuppressive therapy.) Each individual can have only two alleles at each locus, but hundreds of alleles exist in any population. Presumably, the different alleles allow for somewhat different af nities for different antibodies. They may have been selected over evolutionary time to give certain individuals in a population more chances to be able to identify and eliminate foreign substances.
(b) (a) Figure 16.46 A three-dimensional computer model of the antigen-presenting site of an MHC class II protein. The presented peptide is fteen amino acid residues long and is not internally bound at each end. In (a), the view as seen by the T cell; (b) is a side view. The presented peptide is shown in red; the electron surface of the MHC protein is blue. (From: J. H. Brown, et al., Nature
364:33 39, 1993, g. 4, p.35.)
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