Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly
Article Abstract:
Research was conducted to describe the discovery of a proteasome maturation factor that is sensitive to a number of stresses. Characterized by a short in vivo half-life due to degradation, Ump1p plays an important role in coordinating the physical assembly and enzymatic activation of proteasomes. It has a molecular mass of 300-400 kDa and migrates faster in native gels than the 20S proteasome. It also accumulates Ub-protein conjugates while encoding a polypeptide with a calculated molecular mass of 16.8 kDa.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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Dynamin: a molecular motor with pinchase action
Article Abstract:
Various studies have been carried out to examine how the dynamin family of proteins produces a compression force. These studies utilized cell-free systems, collared invaginations and tubular membrane intermediates to determine that the proteins are characterized by three distinct genes supporting several conserved motifs. Researchers are urged to conduct more studies designed to analyze how dynamin assembly and activity are regulated.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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Degradation signal masking by heterodimerization of MAT-alpha-2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway
Article Abstract:
A study was conducted to test whether a1 is degraded in haploid cells. HindIII fragments supporting either the MAT-alpha or MATa loci were subcloned into low and high-copy shuttle plasmids. Results indicated that degradation determinants in a1 and alpha-2 are masked in the heterodimer. Findings also showed that the correlation between alpha-2 and a1 depend on N-terminal coiled-coil interactions.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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