scholarly journals Cyclophilin40 isomerase activity is regulated by a temperature-dependent allosteric interaction with Hsp90

2015 ◽  
Vol 35 (5) ◽  
Author(s):  
Elizabeth A. Blackburn ◽  
Martin A. Wear ◽  
Vivian Landré ◽  
Vikram Narayan ◽  
Jia Ning ◽  
...  
Keyword(s):  
Heat Shock Protein 90 ◽  
Prolyl Isomerase ◽  
Temperature Dependent ◽  
Ppiase Activity ◽  
Peptidyl Prolyl Isomerase ◽  
Isomerase Activity ◽  
C Terminus ◽  
Hsp 90 ◽  
Cyclophilin 40 ◽  
Tpr Domain

Binding the C-terminus of heat shock protein 90 (Hsp 90) to the tetratricopeptide repeat (TPR) domain of cyclophilin 40 (Cyp40) allosterically changes the dynamics of the cyclophilin-active site and reduces peptidyl-prolyl isomerase (PPIase) activity.

scholarly journals Cyclophilin A Peptidyl-Prolyl Isomerase Activity Promotes Zpr1 Nuclear Export

2002 ◽  
Vol 22 (20) ◽  
pp. 6993-7003 ◽  
Author(s):  
Husam Ansari ◽  
Giampaolo Greco ◽  
Jeremy Luban
Keyword(s):  
Nuclear Export ◽  
Biological Function ◽  
Zinc Finger Protein ◽  
Cyclophilin A ◽  
Kinetic Studies ◽  
Wild Type ◽  
Prolyl Isomerase ◽  
Ppiase Activity ◽  
Peptidyl Prolyl Isomerase ◽  
Isomerase Activity

ABSTRACT The peptidyl-prolyl isomerase (PPIase) cyclophilin A (Cpr1p) is conserved from eubacteria to mammals, yet its biological function has resisted elucidation. Unable to identify a phenotype that is suggestive of Cpr1p's function in a cpr1Δ Saccharomyces cerevisiae strain, we screened for CPR1-dependent strains. In all cases, dependence was conferred by mutations in ZPR1, a gene encoding an essential zinc finger protein. CPR1 dependence was suppressed by overexpression of EF1α (a translation factor that binds Zpr1p), Cpr6p (another cyclophilin), or Fpr1p (a structurally unrelated PPIase). Suppression by a panel of cyclophilin A mutants correlated with PPIase activity, confirming the relevance of this activity in CPR1-dependent strains. In CPR1 + cells, wild-type Zpr1p was distributed equally between the nucleus and cytoplasm. In contrast, proteins encoded by CPR1-dependent alleles of ZPR1 accumulated in the nucleus, as did wild-type Zpr1p in cpr1Δ cells. Transport kinetic studies indicated that nuclear export of Zpr1p was defective in cpr1Δ cells, and rescue of this defect correlated with PPIase activity. Our results demonstrate a functional interaction between Cpr1p, Zpr1p, and EF1α, a role for Cpr1p in Zpr1p nuclear export, and a biological function for Cpr1p PPIase activity.

scholarly journals Structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client-maturation state

2021 ◽  
Author(s):  
Kanghyun Lee ◽  
Aye C. Thwin ◽  
Eric Tse ◽  
Stephanie N. Gates ◽  
Daniel R. Southworth
Keyword(s):  
Prolyl Isomerase ◽  
Ppiase Activity ◽  
Peptidyl Prolyl Isomerase ◽  
Recognition Element ◽  
Middle Domain ◽  
Ppiase Domain ◽  
Hsp90 Chaperone ◽  
Client Proteins ◽  
Maturation State ◽  
Tpr Domain

SummaryThe Hsp90 chaperone promotes the folding and activation of hundreds of client proteins in the cell through an ATP-dependent conformational cycle guided by distinct cochaperone regulators. The FKBP51 immunophilin binds Hsp90 with its tetratricopeptide repeat (TPR) domain and catalyzes peptidyl-prolyl isomerase (PPIase) activity during the folding of kinases, nuclear receptors and tau. Here we have determined the cryo-EM structure of the human Hsp90:FKBP51:p23 complex to 3.3 Å that, together with mutagenesis and crosslinking analysis, reveals the basis for cochaperone binding to Hsp90 during client maturation. A helix extension in the TPR functions as a key recognition element, interacting across the Hsp90 C-terminal dimer interface presented in the closed, ATP conformation. The PPIase domain is positioned along the middle domain, adjacent Hsp90 client binding sites, while a single p23 makes stabilizing interactions with the N-terminal dimer. With this architecture, FKBP51 could thereby act on specific client residues presented during Hsp90-catalyzed remodeling.

scholarly journals The Peptidyl-Prolyl Isomerase Activity of SlyD Is Not Required for Maturation of Escherichia coli Hydrogenase

2007 ◽  
Vol 189 (21) ◽  
pp. 7942-7944 ◽  
Author(s):  
Jie Wei Zhang ◽  
Michael R. Leach ◽  
Deborah B. Zamble
Keyword(s):  
Escherichia Coli ◽  
Metal Cluster ◽  
The Other ◽  
Prolyl Isomerase ◽  
Ppiase Activity ◽  
Peptidyl Prolyl Isomerase ◽  
Isomerase Activity ◽  
Hydrogenase Enzymes

ABSTRACT Escherichia coli SlyD, which is involved in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, exhibits several activities including that of a peptidyl-prolyl isomerase (PPIase). Mutations that result in deficient PPIase activity do not produce corresponding decreases in the other activities of SlyD in vitro or in hydrogenase production levels in vivo.

scholarly journals A Functional Analysis of the Cyclophilin Repertoire in the Protozoan Parasite Trypanosoma Cruzi

Biomolecules ◽  
2018 ◽  
Vol 8 (4) ◽  
pp. 132 ◽  
Author(s):  
Alina Perrone ◽  
Natalia Milduberger ◽  
Alicia Fuchs ◽  
Patricia Bustos ◽  
Jacqueline Bua
Keyword(s):  
Trypanosoma Cruzi ◽  
Protozoan Parasite ◽  
The United States ◽  
Prolyl Isomerase ◽  
Ppiase Activity ◽  
Peptidyl Prolyl Isomerase ◽  
Isomerase Activity ◽  
Evolution Of Metabolic Pathways

Trypanosoma cruzi is the etiological agent of Chagas disease. It affects eight million people worldwide and can be spread by several routes, such as vectorborne transmission in endemic areas and congenitally, and is also important in non-endemic regions such as the United States and Europe due to migration from Latin America. Cyclophilins (CyPs) are proteins with enzymatic peptidyl-prolyl isomerase activity (PPIase), essential for protein folding in vivo. Cyclosporin A (CsA) has a high binding affinity for CyPs and inhibits their PPIase activity. CsA has proved to be a parasiticidal drug on some protozoa, including T. cruzi. In this review, we describe the T. cruzi cyclophilin gene family, that comprises 15 paralogues. Among the proteins isolated by CsA-affinity chromatography, we found orthologues of mammalian CyPs. TcCyP19, as the human CyPA, is secreted to the extracellular environment by all parasite stages and could be part of a complex interplay involving the parasite and the host cell. TcCyP22, an orthologue of mitochondrial CyPD, is involved in the regulation of parasite cell death. Our findings on T. cruzi cyclophilins will allow further characterization of these processes, leading to new insights into the biology, the evolution of metabolic pathways, and novel targets for anti-T. cruzi control.

Immunophilin AtFKBP13 Sustains All Peptidyl−Prolyl Isomerase Activity in the Thylakoid Lumen fromArabidopsis thalianaDeficient in AtCYP20-2†

Biochemistry ◽  
2007 ◽  
Vol 46 (33) ◽  
pp. 9432-9442 ◽  
Author(s):  
Anna Edvardsson ◽  
Alexey Shapiguzov ◽  
Ulrika A. Petersson ◽  
Wolfgang P. Schröder ◽  
Alexander V. Vener
Keyword(s):  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Thylakoid Lumen ◽  
Isomerase Activity

scholarly journals FK506-binding protein FklB is involved in biofilm formation through its peptidyl-prolyl isomerase activity

2020 ◽  
Author(s):  
Chrysoula Zografou ◽  
Maria Dimou ◽  
Panagiotis Katinakis
Keyword(s):  
Biofilm Formation ◽  
Negative Regulator ◽  
Cell Length ◽  
Wild Type ◽  
Prolyl Isomerase ◽  
Ppiase Activity ◽  
Peptidyl Prolyl Isomerase ◽  
Knock Out ◽  
E Coli ◽  
The Mean

AbstractFklB is a member of the FK506-binding proteins (FKBPs), a family that consists of five genes in Escherichia coli. Little is known about the physiological and functional role of FklB in bacterial movement. In the present study, FklB knock-out mutant ΔfklB presented an increased swarming and swimming motility and biofilm formation phenotype, suggesting that FklB is a negative regulator of these cellular processes. Complementation with Peptidyl-prolyl isomerase (PPIase)-deficient fklB gene (Y181A) revealed that the defects in biofilm formation were not restored by Y181A, indicating that PPIase activity of FklB is modulating biofilm formation in E. coli. The mean cell length of ΔfklB swarming cells was significantly smaller as compared to the wild-type BW25113. Furthermore, the mean cell length of swarming and swimming wild-type and ΔfklB cells overexpressing fklB or Y181A was considerably larger, suggesting that PPIase activity of FklB plays a role in cell elongation and/or cell division. A multi-copy suppression assay demonstrated that defects in motility and biofilm phenotype were compensated by overexpressing sets of PPIase-encoding genes. Taken together, our data represent the first report demonstrating the involvement of FklB in cellular functions of E. coli.

scholarly journals The major peptidyl-prolyl isomerase activity in thylakoid lumen of plant chloroplasts belongs to a novel cyclophilin TLP20

FEBS Letters ◽  
2003 ◽  
Vol 542 (1-3) ◽  
pp. 137-141 ◽  
Author(s):  
Anna Edvardsson ◽  
Said Eshaghi ◽  
Alexander V Vener ◽  
Bertil Andersson
Keyword(s):  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Thylakoid Lumen ◽  
Isomerase Activity
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