NDLI: Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway

Please wait, while we are loading the content...

Exploring the interaction between the protein kinase A catalytic subunit and caveolin-1 scaffolding domain with shotgun scanning, oligomer complementation, NMR, and docking

The solution structure of the methylated form of the N-terminal 16-kDa domain of Escherichia coli Ada protein

Solution structure and backbone dynamics of an N-terminal ubiquitin-like domain in the GLUT4-regulating protein, TUG

A general model of G protein-coupled receptor sequences and its application to detect remote homologs

Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure

Methionine oxidation of monomeric λ repressor: The denatured state ensemble under nondenaturing conditions

Physical characterization of MxiH and PrgI, the needle component of the type III secretion apparatus from Shigella and Salmonella

On the precision of experimentally determined protein folding rates and φ-values

Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics

Automated extraction of backbone deuteration levels from amide H/2H mass spectrometry experiments

Temperature-induced reversible conformational change in the first 100 residues of α-synuclein

Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation

Global structural rearrangement of the cell penetrating ribonuclease colicin E3 on interaction with phospholipid membranes

Solution structure of PcFK1, a spider peptide active against Plasmodium falciparum

Monitoring protein aggregation during thermal unfolding in circular dichroism experiments

Site-specific labeling of proteins for single-molecule FRET by combining chemical and enzymatic modification

The early history of the ubiquitin field

Year: 2006, Volume: 15, Issue: 2

Year: 2006, Volume: 15, Issue: 1

Year: 2005, Volume: 14

Year: 2004, Volume: 13

Year: 2003, Volume: 12

Year: 2002, Volume: 11

Year: 2001, Volume: 10

Year: 2000, Volume: 9

Year: 1999, Volume: 8

Year: 1998, Volume: 7

Year: 1997, Volume: 6

Year: 1996, Volume: 5

Year: 1995, Volume: 4

Year: 1994, Volume: 3

Year: 1993, Volume: 2

Year: 1992, Volume: 1

Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway

Content Provider	PubMed Central
Author	Fisher, Adam C. Kim, Woojin Delisa, Matthew P.
Abstract	One of the most vexing problems facing structural genomics efforts and the biotechnology enterprise in general is the inability to efficiently produce functional proteins due to poor folding and insolubility. Additionally, protein misfolding and aggregation has been linked to a number of human diseases, such as Alzheimer’s. Thus, a robust cellular assay that allows for direct monitoring, manipulation, and improvement of protein folding could have a profound impact. We report the development and characterization of a genetic selection for protein folding and solubility in living bacterial cells. The basis for this assay is the observation that protein transport through the bacterial twin-arginine translocation (Tat) pathway depends on correct folding of the protein prior to transport. In this system, a test protein is expressed as a tripartite fusion between an N-terminal Tat signal peptide and a C-terminal TEM1 β-lactamase reporter protein. We demonstrate that survival of Escherichia coli cells on selective medium expressing a Tat-targeted test protein/β-lactamase fusion correlates with the solubility of the test protein. Using this assay, we isolated solubility-enhanced variants of the Alzheimer’s Aβ42 peptide from a large combinatorial library of Aβ42 sequences, thereby confirming that our assay is a highly effective selection tool for soluble proteins. By allowing the bacterial Tat pathway to exert folding quality control on expressed target protein sequences, we have generated a powerful tool for monitoring protein folding and solubility in living cells, for molecular engineering of solubility-enhanced proteins or for the isolation of factors and/or cellular conditions that stabilize aggregation-prone proteins.
Related Links	http://dx.doi.org/10.1110/ps.051902606
Ending Page	458
Page Count	10
Starting Page	449
File Format	PDF
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	3
Volume Number	15
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2006-02-01
Access Restriction	Open
Rights Holder	Cold Spring Harbor Laboratory Press
Subject Keyword	Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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

Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway.

Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway

Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo–designed heme protein

The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding

Genetic and Biochemical Analysis of the Twin-Arginine Translocation Pathway in Halophilic Archaea

Involvement of the twin-arginine translocation system in protein secretion via the type II pathway

Role of the Twin-Arginine Translocation Pathway in Staphylococcus ▿ †

Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat)

Twin-Arginine Translocation Pathway in Streptomyces lividans

Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway

Similar Documents

Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway.

Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway

Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo–designed heme protein

The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding

Genetic and Biochemical Analysis of the Twin-Arginine Translocation Pathway in Halophilic Archaea

Involvement of the twin-arginine translocation system in protein secretion via the type II pathway

Role of the Twin-Arginine Translocation Pathway in Staphylococcus ▿ †

Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat)

Twin-Arginine Translocation Pathway in Streptomyces lividans

Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway