Einzeltreffer — DigiBib

Background: Peptidyl-prolyl isomerases (PPIases) are enzymes that assist in the folding of newly-synthesized proteins and regulate the stability, localization, and activity of mature proteins. They do so by catalyzing reversible (cis-trans) rotation about the peptide bond that precedes proline, inducing conformational changes in target proteins.

Scope of Review: This review will discuss how PPIases regulate gene transcription by controlling the activity of (1) DNA-binding transcription regulatory proteins, (2) RNA polymerase II, and (3) chromatin and histone modifying enzymes.

Major Conclusions: Members of each family of PPIase (cyclophilins, FKBPs, and parvulins) regulate gene transcription at multiple levels. In all but a few cases, the exact mechanisms remain elusive. Structure studies, development of specific inhibitors, and new methodologies for studying cis/trans isomerization in vivo represent some of the challenges in this new frontier that merges two important fields.

General Significance: Prolyl isomerases have been found to play key regulatory roles in all phases of the transcription process. Moreover, PPIases control upstream signaling pathways that regulate gene-specific transcription during development, hormone response and environmental stress. Although transcription is often rate-limiting in the production of enzymes and structural proteins, post-transcriptional modifications are also critical, and PPIases play key roles here as well (see other reviews in this issue). This article is part of a Special Issue entitled Proline-directed Foldases: Cell Signaling Catalysts and Drug Targets.

Titel:	Prolyl isomerases in gene transcription.
Autor/in / Beteiligte Person:	Hanes, SD
Zeitschrift:	Biochimica et biophysica acta, Jg. 1850 (2015-10-01), Heft 10, S. 2017-34
Veröffentlichung:	Amsterdam : Elsevier Pub. Co., 2015
Medientyp:	academicJournal
ISSN:	0006-3002 (print)
DOI:	10.1016/j.bbagen.2014.10.028
Schlagwort:	Animals Histones metabolism Humans Protein Processing, Post-Translational physiology Chromatin metabolism DNA-Binding Proteins metabolism Peptidylprolyl Isomerase metabolism RNA Polymerase II metabolism Transcription, Genetic physiology
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Review Language: English [Biochim Biophys Acta] 2015 Oct; Vol. 1850 (10), pp. 2017-34. <i>Date of Electronic Publication: </i>2014 Oct 31. MeSH Terms: Chromatin / metabolism ; DNA-Binding Proteins / metabolism ; Peptidylprolyl Isomerase / metabolism ; RNA Polymerase II / metabolism ; Transcription, Genetic / *physiology ; Animals ; Histones / metabolism ; Humans ; Protein Processing, Post-Translational / physiology References: Mol Cell. 2009 Nov 25;36(4):541-6. (PMID: 19941815) ; Expert Rev Mol Med. 2011;13:e21. (PMID: 21682951) ; Cell Res. 2010 Mar;20(3):357-66. (PMID: 20142844) ; Science. 2011 Apr 1;332(6025):99-103. (PMID: 21454787) ; Mol Cell Biol. 2009 Jun;29(11):2925-34. (PMID: 19332564) ; J Cell Biol. 2013 Oct 14;203(1):57-71. 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(PMID: 8606777) Grant Information: R01 GM055108 United States GM NIGMS NIH HHS; R01-GM55108 United States GM NIGMS NIH HHS Contributed Indexing: Keywords: Ess1; Histone modification; Immunophilins; Pin1; RNA polymerase II CTD; Transcription regulation Substance Nomenclature: 0 (Chromatin) ; 0 (DNA-Binding Proteins) ; 0 (Histones) ; EC 2.7.7.- (RNA Polymerase II) ; EC 5.2.1.8 (Peptidylprolyl Isomerase) Entry Date(s): Date Created: 20141203 Date Completed: 20151109 Latest Revision: 20181113 Update Code: 20240513 PubMed Central ID: PMC4417086

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Prolyl isomerases in gene transcription.