Peptidyl-prolyl isomerases: a new twist to transcription.
Peptidyl-prolyl isomerases (PPIs) catalyse the cis-trans isomerisation of peptide bonds N-terminal to proline residues in polypeptide chains. They have roles in the folding of newly synthesised proteins and in the function of the immune system. In addition, members of the parvulin-like family of PPIs have been implicated in cell cycle control. Their activity is directed by the prior phosphorylation of target proteins in both yeast and mammalian cells. More recent data have illustrated that they may also influence other nuclear events. This review examines PPI activity in the context of eukaryotic transcriptional regulation. The findings are consistent with a two-step model of conformational control, in which the outcome depends on the transcription factor involved.
Shaw
Peter E
PE
School of Biomedical Sciences and Institute of Cell Signalling, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK. peter.shaw@nottingham.ac.uk
D000818:Animals; D020868:Gene Silencing / Q000502:physiology; D006801:Humans; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019696:Peptidylprolyl Isomerase / Q000502:physiology*; D012319:RNA Polymerase II / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism; D014158:Transcription, Genetic
D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D014157:Transcription Factors; D012319:RNA Polymerase II; C000606846:PIN1 protein, human; D019696:Peptidylprolyl Isomerase