Functional Replacement of the Essential ESS1 in Yeast by the Plant Parvulin DlPar13

A functionally Pin1-like peptidyl-prolyl cis/trans isomerase (PPIase 1 ) was isolated from proembryogenic masses (PEMs) of Digitalis lanata according to its enzymatic activity. Partial sequence analysis of the purified enzyme ( Dl Par13) revealed sequence homology to members of the parvulin family o...

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Veröffentlicht in:	The Journal of biological chemistry 2001-04, Vol.276 (17), p.13524-13529
Hauptverfasser:	Metzner, M, Stoller, G, Rücknagel, K P, Lu, K P, Fischer, G, Luckner, M, Küllertz, G
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Blotting, Western Cell Nucleus - metabolism Cloning, Molecular Cytosol - metabolism D1Par13 enzyme Digitalis - enzymology Digitalis lanata DlPar13 protein DNA, Complementary - metabolism Enzyme Inhibitors - pharmacology Escherichia coli - chemistry Escherichia coli Proteins ESS1 gene Ess1 protein Genetic Complementation Test Humans isomerase Kinetics Molecular Sequence Data Mutation Naphthoquinones - pharmacology NIMA-Interacting Peptidylprolyl Isomerase Peptidylprolyl Isomerase - chemistry Peptidylprolyl Isomerase - metabolism Peptidylprolyl Isomerase - physiology Phenotype Phosphoserine - metabolism Phosphothreonine - metabolism PIN1 gene Plant Proteins Plants, Medicinal Plants, Toxic proembryogenic masses Protein Structure, Tertiary Reverse Transcriptase Polymerase Chain Reaction Saccharomyces cerevisiae Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Subcellular Fractions - metabolism Substrate Specificity Temperature Time Factors
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