Murine cyclophilin-S1: a variant peptidyl-prolyl isomerase with a putative signal sequence expressed in differentiating F9 cells.

Abstract

Fractionation of differentiating murine teratocarcinoma F9 cells and extraction of the nuclear/microsomal pellets with ethidium bromide led to the purification and microsequencing of the protein mCyP-S1, a novel cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase (PPIase). mCyP-S1 is a new member of the cyclophilin class of proteins. Cloning and sequencing of the mCyP-S1 cDNA revealed extended coding capacity for a putative N-terminal signal sequence, suggesting processing of mCyP-S1 during intracellular translocation across the membrane of the endoplasmic reticulum. mCyP-S1 is abundantly expressed in a variety of mouse organ tissues and its mRNA levels increase during F9 cell differentiation. Specific subcellular localization of PPIases is postulated to contribute to functional specificities of this class of enzymes.

• Authors: A Schumacher, H Schröter, G Multhaup, A Nordheim
• Journal: Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 1129 Issue 1 Pg. 13-22 (Dec 02 1991) ISSN: 0006-3002 [Print] Netherlands
• PMID: 1756174 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Carrier Proteins
• Cyclosporins
• Protein Sorting Signals
• Amino Acid Isomerases
• Cyclophilins
• cyclophilin-S1
• Peptidylprolyl Isomerase

Topics

• Amino Acid Isomerases (genetics)
• Amino Acid Sequence
• Animals
• Base Sequence
• Blotting, Southern
• Carrier Proteins (genetics)
• Cell Differentiation (genetics)
• Cloning, Molecular
• Cyclophilins
• Cyclosporins (genetics)
• Gene Expression (genetics)
• Mice (genetics)
• Molecular Sequence Data
• Peptidylprolyl Isomerase
• Protein Sorting Signals (genetics)
• Sequence Alignment
• Sequence Homology, Nucleic Acid
• Tumor Cells, Cultured