|
|
|
Research Papers
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
Abstract
The highly conserved and ubiquitously expressed mouse gene H < beta > 58, identified through insertional mutagenesis, has been shown to be essential for early postimplantation development in mouse, but the mechanism by which it acts is unknown (Radice et al. 1991; Lee et al. 1992). We report here the identification of a yeast gene related to the H < beta > 58 gene and provide biochemical and genetic evidence for its function within the cell. The gene, PEP8, plays a role in the delivery of proteins to the vacuole. Disruption of the gene did not affect cell viability. However, the disruptants were shown to have a defect in the processing of the soluble vacuolar proteases but not the membrane vacuolar hydrolases. The processing defect appeared to be a consequence of the inability of the soluble vacuolar hydrolase to reach the vacuole. Although a small amount of the vacuolar precursors was mis-sorted to the extracellular medium, mis-sorting did not appear to be the primary defect in these cells. Pep8p was identified by epitope tagging of the protein. Biochemical fractionation indicated that the protein was peripherally bound to membranes. Immuno-gold electron microscopy indicated that the Pep8p localized to vacuolar membranes. Complementation experiments with the mouse H < beta > 58 cDNA revealed that a Pep8p-H < beta > 58 fusion protein in which the carboxy-terminal 85 amino acids of Pep8p were replaced by the carboxy-terminal 115 amino acids of H < beta > 58 was functional.(ABSTRACT TRUNCATED AT 250 WORDS)
This article has been cited by other articles:
![]() |
T. Shimada, Y. Koumoto, L. Li, M. Yamazaki, M. Kondo, M. Nishimura, and I. Hara-Nishimura AtVPS29, a Putative Component of a Retromer Complex, is Required for the Efficient Sorting of Seed Storage Proteins Plant Cell Physiol., September 1, 2006; 47(9): 1187 - 1194. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. V. Reddy and M. N.J. Seaman Vps26p, a Component of Retromer, Directs the Interactions of Vps35p in Endosome-to-Golgi Retrieval Mol. Biol. Cell, October 1, 2001; 12(10): 3242 - 3256. [Abstract] [Full Text] [PDF] |
||||
![]() |
V. Rider, S. R. Jones, R. T. Foster, and K. Imakawa Changes in the Temporal and Spatial Expression of H{beta}58 During Formation and Maturation of the Chorioallantoic Placenta in the Rat Biol Reprod, December 1, 2000; 63(6): 1735 - 1746. [Abstract] [Full Text] |
||||
![]() |
C. R. Haft, M. d. l. L. Sierra, R. Bafford, M. A. Lesniak, V. A. Barr, and S. I. Taylor Human Orthologs of Yeast Vacuolar Protein Sorting Proteins Vps26, 29, and 35: Assembly into Multimeric Complexes Mol. Biol. Cell, December 1, 2000; 11(12): 4105 - 4116. [Abstract] [Full Text] |
||||
![]() |
M. N.J. Seaman, J. Michael McCaffery, and S. D. Emr A Membrane Coat Complex Essential for Endosome-to-Golgi Retrograde Transport in Yeast J. Cell Biol., August 10, 1998; 142(3): 665 - 681. [Abstract] [Full Text] [PDF] |
||||
![]() |
O. Kerscher, J. Holder, M. Srinivasan, R. S. Leung, and R. E. Jensen The Tim54p-Tim22p Complex Mediates Insertion of Proteins into the Mitochondrial Inner Membrane J. Cell Biol., December 29, 1997; 139(7): 1663 - 1675. [Abstract] [Full Text] [PDF] |
||||