Prolyl Isomerases Show Low Sequence Specificity toward the Residue Following the Proline

Schmidpeter, Philipp A. M.; Jahreis, Günther; Geitner, Anne-Juliane; Schmid, Franz X.

doi:10.1021/bi200442q

Cited by 14 publications

(14 citation statements)

References 49 publications

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“…This property is generally true for all three prolyl isomerase families (72,73), except for the protein Pin1 which recognizes a phosphorylated serine or threonine before the proline residue (74). Instead, cellular targets appear to be defined by domains such as the BTHB that limit the protein to a specific location or biomolecular complex.…”

Section: Discussionmentioning

confidence: 99%

The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module

Dilworth¹,

Upadhyay²,

Bonnafous³

et al. 2017

Nucleic Acids Research

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Prolyl isomerases are defined by a catalytic domain that facilitates the cis–trans interconversion of proline residues. In most cases, additional domains in these enzymes add important biological function, including recruitment to a set of protein substrates. Here, we report that the N-terminal basic tilted helix bundle (BTHB) domain of the human prolyl isomerase FKBP25 confers specific binding to double-stranded RNA (dsRNA). This binding is selective over DNA as well as single-stranded oligonucleotides. We find that FKBP25 RNA-association is required for its nucleolar localization and for the vast majority of its protein interactions, including those with 60S pre-ribosome and early ribosome biogenesis factors. An independent mobility of the BTHB and FKBP catalytic domains supports a model by which the N-terminus of FKBP25 is anchored to regions of dsRNA, whereas the FKBP domain is free to interact with neighboring proteins. Apart from the identification of the BTHB as a new dsRNA-binding module, this domain adds to the growing list of auxiliary functions used by prolyl isomerases to define their primary cellular targets.

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Section: Discussionmentioning

confidence: 99%

The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module

Dilworth¹,

Upadhyay²,

Bonnafous³

et al. 2017

Nucleic Acids Research

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“…With its k cat /K m value of 3 ϫ 10 3 mM Ϫ1 s Ϫ1 for the Leu-Pro peptide, PrsA shows an activity that is 1000-and 10-fold higher than the activities of human parvulin 14 and E. coli SurA, respectively, and only 10-fold lower than the activity of E. coli parvulin 10, which is the most active parvulin known to date (48). In its substrate specificity with a preference for hydrophobic residues preceding proline, PrsA resembles other bacterial parvulin homologues (49,50).…”

Section: Catalysis Of Prolyl Isomerization By Prsa In Peptides Andmentioning

confidence: 94%

Dimeric Structure of the Bacterial Extracellular Foldase PrsA

Jakob

Koch

Burmann

et al. 2015

Journal of Biological Chemistry

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Background: PrsA is a foldase for secreted proteins and pathogenicity factors in Gram-positive bacteria. Results: Crystallographic, enzymatic, and NMR spectroscopic analysis provide insights to PrsA function. Conclusion: Substrate peptides interact around a unique crevice generated by PrsA dimerization via its chaperone-like domain. Significance: The comprehensive characterization of PrsA promotes its utilization as foldase and drug target.

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“…FKBP domains often show high activity towards peptide substrates, but the catalysis of proline-limited protein folding is usually weak. The folding activity can be dramatically increased in the presence of a chaperone domain (Knappe et al, 2007;Schmidpeter et al, 2011;Geitner and Schmid, 2012). We determined the sequence specificities of the three TFs by using five fluorescent tetrapeptides of the type aminobenzoyl-Ala-Xaa-Pro-Phe-p-nitroanilide (Abz-AXPF-pNA) (Zoldak et al, 2009) with amino acids of different chemical character preceding the proline (i.e.…”

Section: Sequence Specificity Of the Ppiase Domain Of The Three Tfsmentioning

confidence: 99%

Functional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures

Godin-Roulling

Schmidpeter

Schmid

et al. 2015

Environmental Microbiology

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Summary Trigger factor (TF) is the first molecular chaperone interacting cotranslationally with virtually all nascent polypeptides synthesized by the ribosome in bacteria. Thermal adaptation of chaperone function was investigated in TFs from the Antarctic psychrophile Pseudoalteromonas haloplanktis, the mesophile Escherichia coli and the hyperthermophile Thermotoga maritima. This series covers nearly all temperatures encountered by bacteria. Although structurally homologous, these TFs display strikingly distinct properties that are related to the bacterial environmental temperature. The hyperthermophilic TF strongly binds model proteins during their folding and protects them from heat‐induced misfolding and aggregation. It decreases the folding rate and counteracts the fast folding rate imposed by high temperature. It also functions as a carrier of partially folded proteins for delivery to downstream chaperones ensuring final maturation. By contrast, the psychrophilic TF displays weak chaperone activities, showing that these functions are less important in cold conditions because protein folding, misfolding and aggregation are slowed down at low temperature. It efficiently catalyses prolyl isomerization at low temperature as a result of its increased cellular concentration rather than from an improved activity. Some chaperone properties of the mesophilic TF possibly reflect its function as a cold shock protein in E. coli.

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Prolyl Isomerases Show Low Sequence Specificity toward the Residue Following the Proline

Cited by 14 publications

References 49 publications

The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module

The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module

Dimeric Structure of the Bacterial Extracellular Foldase PrsA

Functional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures

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