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By Frank J. Dixon

Learn Institute of Scripps hospital, los angeles Jolla. study within the box. For investigators. 19 participants, 6 U.S.

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Koszinowski, U. , and Kloetzel, P. M. Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20s proteasomes. J. Exp. Med. 179,901-909. Brown, M. , and Monaco, J. J. (1993). MHC-linked low-molecular mass polypeptide subunits define distinct subsets of proteasomes. Implications for divergent function among distinct proteasome subsets. J. Immunol. 151, 1193-1204. , and Townsend, A. (1995). Genes encoded in the major histocompatibility complex affecting the generation of peptides for TAP transport.

Intriguingly, several subunits of both the 20s and 26s proteasomes and PA28a have a unique segment, named a KEKE motif by Realini et al. (1994b); it consists of a very hydrophilic domain rich in “alternating” lysine (positive) and glutamate (negative) residues. A similar sequence is present in a variety of proteins such as heat-shock proteins and Ca2+-bindingER proteins. , 1994b). Therefore, the molecules responsible for processing and intracellular transportation of antigenic peptides may be associated physically through the KEKE motif, as shown in the hypothetical mode in Fig.

Depending on the orientation of the signals, the rearrangement can lead to either a deletion or an inversion of the intervening DNA. In the most common arrays at the antigen receptor loci, the coding joint is retained in the chromosome and a circular DNA molecular containing the signal joint is excised and subsequently lost from the cells. The alternative naturally occurring arrangement of signals leads to an inversion. , 1990). These segments are used in expressed IgK genes. , 1986). The signal sequences are the only recognition sites strictly required for recombination; coding segments can be replaced by other DNA and joining still occurs at the signal border.

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