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Start Over Author "Julia Kipper" Publisher published by elsevier b.v.
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1. PRE3, highly homologous to the human major histocompatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolyzing activity

Author

Dieter H. Wolf, Roland Gückel, Julia Kipper, Cordula Enenkel, Heike Lehmann, and Wolfgang Hilt

Subjects
Proteasome Endopeptidase Complex, Saccharomyces cerevisiae Proteins, Protein subunit, Molecular Sequence Data, Biophysics, Glutamic Acid, Saccharomyces cerevisiae, Major histocompatibility complex, Biochemistry, Homology (biology), Proteolysis (yeast), Fungal Proteins, Major Histocompatibility Complex, Glutamates, Structural Biology, Multienzyme Complexes, Antigen processing (human MHC), Endopeptidases, Genetics, Gene family, Humans, Amino Acid Sequence, Molecular Biology, Gene, biology, Base Sequence, Sequence Homology, Amino Acid, Proteasome, Antigen processing, Hydrolysis, Proteins, Cell Biology, Complementation, Cysteine Endopeptidases, biology.protein, Peptides
Abstract

20S proteasomes are multifunctional proteinase complexes ubiquitous in eucaryotes. We have cloned the yeast PRE3 gene by complementation of the pre3-2 mutation, which leads to a defect in the peptidylglutamyl-peptide hydrolyzing activity of the 20S proteasome. The PRE3 gene, a beta-type member of the proteasomal gene family, is essential for cellular life and codes for a 193-amino acid proteasomal subunit with a predicted molecular mass of 21.2 kDa. The Pre3 protein shows striking homology to the human proteasome subunits Hs delta and Lmp2 (Ring12). Lmp2 is encoded in the major histocompatibility complex class II region implicating proteasomes in antigen processing.

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