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Molecular Characterization of a Novel Mammalian DnaJ-Like Sec63p Homolog
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Markus H. Skowronek
Veröffentlicht/Copyright:
1. Juni 2005
Abstract
We identified a human cDNA sequence encoding a polypeptide of 760 amino acids that shares 53% homology and 25.6% identity with the yeast DnaJ-like endoplasmic reticulum (ER) translocon component Sec63p. Three epitope-specific antisera revealed a protein of an apparent molecular mass of 83 kDa, both in human cell extracts and in dog pancreatic microsomes. Biochemical analyses show that it is an integral membrane protein of the rough ER, which has the DnaJ domain located in the ER lumen. The novel Sec63 protein could thus represent a key component of the mammalian ER protein translocation machinery.
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Published Online: 2005-06-01
Published in Print: 1999-09-13
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
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Artikel in diesem Heft
- Execution of Apoptosis: Converging or Diverging Pathways?
- Two Highly Related Homeodomain Proteins, Nkx5-1 and Nkx5-2, Display Different DNA Binding Specificities
- The Janus Face of the Archaeal Cdc48/p97 Homologue VAT: Protein Folding versus Unfolding
- Functional Characterization of an Extremely Thermophilic ATPase in Membranes of the Crenarchaeon Acidianus ambivalens
- On the Lysosomal Degradation of Neurofibromin and Its Phosphorylation in Cultured Melanocytes
- Rat Muscle Fructose-1,6-Bisphosphatase: Cloning of the cDNA, Expression of the Recombinant Enzyme, and Expression Analysis in Different Tissues
- Catalase-Peroxidase from the Cyanobacterium Synechocystis PCC 6803: Cloning, Overexpression in Escherichia coli, and Kinetic Characterization
- Expression of Plasma Prekallikrein mRNA in Human Nonhepatic Tissues and Cell Lineages Suggests Special Local Functions of the Enzyme
- Biochemical Characterization of the Catalytic Domain of Membrane-Type 4 Matrix Metalloproteinase
- Fluorometric Microassays for the Determination of Cathepsin L and Cathepsin S Activities in Tissue Extracts
- The Role of Protein Phosphatase 2A Catalytic Subunit Cα in Embryogenesis: Evidence from Sequence Analysis and Localization Studies
- DNA Binding of Myc/Max/Mad Network Complexes to Oligonucleotides Containing Two E Box Elements: c-Myc/Max Heterodimers Do Not Bind DNA Cooperatively
- Tight Interaction between Densely Methylated DNA Fragments and the Methyl-CpG Binding Domain of the Rat MeCP2 Protein Attached to a Solid Support
- Molecular Characterization of a Novel Mammalian DnaJ-Like Sec63p Homolog
