NDLI: Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone

Content Provider	Journal of Biological Chemistry (JBC)
Author	Kawagoe, Soichiro Nakagawa, Hiroshi Kumeta, Hiroyuki Ishimori, Koichiro Saio, Tomohide
Abstract	Molecular chaperones often possess functional modules that are specialized in assisting the formation of specific structural elements, such as a disulfide bridges and peptidyl–prolyl bonds in cis form, in the client protein. A ribosome-associated molecular chaperone trigger factor (TF), which has a peptidyl–prolyl cis/trans isomerase (PPIase) domain, acts as a highly efficient catalyst in the folding process limited by peptidyl–prolyl isomerization. Herein we report a study on the mechanism through which TF recognizes the proline residue in the unfolded client protein during the cis/trans isomerization process. The solution structure of TF in complex with the client protein showed that TF recognizes the proline-aromatic motif located in the hydrophobic stretch of the unfolded client protein through its conserved hydrophobic cleft, which suggests that TF preferentially accelerates the isomerization of the peptidyl–prolyl bond that is eventually folded into the core of the protein in its native fold. Molecular dynamics simulation revealed that TF exploits the backbone amide group of Ile195 to form an intermolecular hydrogen bond with the carbonyl oxygen of the amino acid residue preceding the proline residue at the transition state, which presumably stabilizes the transition state and thus accelerates the isomerization. The importance of such intermolecular hydrogen-bond formation during the catalysis was further corroborated by the activity assay and NMR relaxation analysis.
Related Links	http://www.jbc.org/content/293/39/15095.abstract
Ending Page	15106
Starting Page	15095
Page Count	12
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	39
Volume Number	293
DOI	10.1074/jbc.RA118.003579
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2018-09-28
Access Restriction	Open
Subject Keyword	Molecular chaperone Prolyl isomerase Molecular dynamics Protein folding Structure-function Nuclear magnetic resonance (NMR) Hydrophobic interaction Peptidyl-prolyl isomerase domain Trigger factor Molecular Biophysics
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

NMR assignments of the peptidyl-prolyl cis–trans isomerase domain of trigger factor from E. coli

Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline Isomerization

Trigger Factor Peptidyl-prolyl cis/trans Isomerase Activity Is Not Essential for the Folding of Cytosolic Proteins in Escherichia coli

Proline Isomerization as a Key Determinant for Hsp90-Toxin Interactions

Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18).

Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline Isomerization*

Proline Isomerization Is Unlikely to Be the Cause of Slow Annealing and Reactivation during the Folding of Alkaline Phosphatase

Editorial: Phosphorylation-Dependent Peptidyl-Prolyl Cis/Trans Isomerase PIN1

A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.

Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone

Similar Documents

NMR assignments of the peptidyl-prolyl cis–trans isomerase domain of trigger factor from E. coli

Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline Isomerization

Trigger Factor Peptidyl-prolyl cis/trans Isomerase Activity Is Not Essential for the Folding of Cytosolic Proteins in Escherichia coli

Proline Isomerization as a Key Determinant for Hsp90-Toxin Interactions

Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18).

Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline Isomerization*

Proline Isomerization Is Unlikely to Be the Cause of Slow Annealing and Reactivation during the Folding of Alkaline Phosphatase

Editorial: Phosphorylation-Dependent Peptidyl-Prolyl Cis/Trans Isomerase PIN1

A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.

Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone