The complete primary structure of mouse 20S proteasomes

被引:0
|
作者
Laura A. Elenich
D. Nandi
A. Elizabeth Kent
T. Scott McCluskey
M. Cruz
Mohan N. Iyer
Elaine C. Woodward
Christopher W. Conn
Amber L. Ochoa
David B. Ginsburg
J. J. Monaco
机构
[1] Howard Hughes Medical Institute,
[2] and Departments of Molecular Genetics and Cell Biology,undefined
[3] University of Cincinnati,undefined
[4] 231 Bethesda Avenue,undefined
[5] Cincinnati,undefined
[6] OH 45267-0524,undefined
[7] USA e-mail: monacojj@ucmail.uc.edu,undefined
[8] Tel.: +1-513-5585521,undefined
[9] Fax: +1-513-5585530,undefined
[10] Department of Microbiology and Immunology,undefined
[11] Virginia Commonwealth University,undefined
[12] Richmond,undefined
[13] VA 23298-0678,undefined
[14] USA,undefined
来源
Immunogenetics | 1999年 / 49卷
关键词
Key words Proteasome; Antigen processing; Multicatalytic proteinase; Proteolysis; Protein degradation;
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学科分类号
摘要
 The proteasome is a large multicatalytic proteinase that plays a role in the generation of peptides for presentation by major histocompatibility complex class I molecules. The 20S proteolytic core of mammalian proteasomes is assembled from a group of 17 protein subunits that generate a distinctive pattern of spots upon two-dimensional gel electrophoresis. The genes for most of these subunits have been cloned from humans and rats. We isolated cDNA clones for the mouse orthologues of ten of the subunits [PSMA1 (C2), PSMA2 (C3), PSMA3 (C8), PSMA4 (C9), PSMA5 (ZETA), PSMA6 (IOTA), PSMA7 (C6-I), PSMB2 (C7-I), PSMB3 (C10-II), and PSMB5 (X)] to complete the cloning of all of the mouse subunits. Using antisera raised against these subunits or their orthologues, we verified the identity of these proteins by two-dimensional NEPHGE-PAGE.
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页码:835 / 842
页数:7
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