Literature DB >> 18836021

The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.

Mónica Martínez-Alonso1, Nuria González-Montalbán, Elena García-Fruitós, Antonio Villaverde.   

Abstract

We have observed that a soluble recombinant green fluorescent protein produced in Escherichia coli occurs in a wide conformational spectrum. This results in differently fluorescent protein fractions in which morphologically diverse soluble aggregates abound. Therefore, the functional quality of soluble versions of aggregation-prone recombinant proteins is defined statistically rather than by the prevalence of a canonical native structure.

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Year:  2008        PMID: 18836021      PMCID: PMC2592911          DOI: 10.1128/AEM.01446-08

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  19 in total

1.  The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures.

Authors:  Andrea Vera; Nuria González-Montalbán; Anna Arís; Antonio Villaverde
Journal:  Biotechnol Bioeng       Date:  2007-04-15       Impact factor: 4.530

2.  Localization of functional polypeptides in bacterial inclusion bodies.

Authors:  Elena García-Fruitós; Anna Arís; Antonio Villaverde
Journal:  Appl Environ Microbiol       Date:  2006-11-03       Impact factor: 4.792

3.  Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to alpha-D-glucose-1-phosphate.

Authors:  Jozef Nahálka
Journal:  J Ind Microbiol Biotechnol       Date:  2007-12-18       Impact factor: 3.346

4.  Recombinant protein solubility - does more mean better?

Authors:  Nuria González-Montalbán; Elena García-Fruitós; Antonio Villaverde
Journal:  Nat Biotechnol       Date:  2007-07       Impact factor: 54.908

5.  A crosslinked inclusion body process for sialic acid synthesis.

Authors:  Jozef Nahálka; Alica Vikartovská; Eva Hrabárová
Journal:  J Biotechnol       Date:  2008-03-20       Impact factor: 3.307

6.  Divergent genetic control of protein solubility and conformational quality in Escherichia coli.

Authors:  Elena García-Fruitós; Mónica Martínez-Alonso; Nuria Gonzàlez-Montalbán; Minoska Valli; Diethard Mattanovich; Antonio Villaverde
Journal:  J Mol Biol       Date:  2007-09-08       Impact factor: 5.469

7.  Properties of soluble fusions between mammalian aspartic proteinases and bacterial maltose-binding protein.

Authors:  D Sachdev; J M Chirgwin
Journal:  J Protein Chem       Date:  1999-01

8.  Encapsulation of Trigonopsis variabilis D-amino acid oxidase and fast comparison of the operational stabilities of free and immobilized preparations of the enzyme.

Authors:  Jozef Nahalka; Iskandar Dib; Bernd Nidetzky
Journal:  Biotechnol Bioeng       Date:  2008-02-01       Impact factor: 4.530

9.  Characterization of the aggregates formed during recombinant protein expression in bacteria.

Authors:  Andrea Schrödel; Ario de Marco
Journal:  BMC Biochem       Date:  2005-05-31       Impact factor: 4.059

10.  Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli.

Authors:  Hans Peter Sørensen; Kim Kusk Mortensen
Journal:  Microb Cell Fact       Date:  2005-01-04       Impact factor: 5.328

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  13 in total

1.  Rehosting of bacterial chaperones for high-quality protein production.

Authors:  Mónica Martínez-Alonso; Verónica Toledo-Rubio; Rob Noad; Ugutz Unzueta; Neus Ferrer-Miralles; Polly Roy; Antonio Villaverde
Journal:  Appl Environ Microbiol       Date:  2009-10-09       Impact factor: 4.792

2.  Cross-system excision of chaperone-mediated proteolysis in chaperone-assisted recombinant protein production.

Authors:  Mónica Martínez-Alonso; Antonio Villaverde; Neus Ferrer-Miralles
Journal:  Bioeng Bugs       Date:  2009-12-29

3.  Engineering building blocks for self-assembling protein nanoparticles.

Authors:  Esther Vázquez; Antonio Villaverde
Journal:  Microb Cell Fact       Date:  2010-12-30       Impact factor: 5.328

4.  Recombinant Protein Production and Purification of Insoluble Proteins.

Authors:  Neus Ferrer-Miralles; Paolo Saccardo; José Luis Corchero; Elena Garcia-Fruitós
Journal:  Methods Mol Biol       Date:  2022

5.  Components of the E. coli envelope are affected by and can react to protein over-production in the cytoplasm.

Authors:  Riccardo Villa; Marina Lotti; Pietro Gatti-Lafranconi
Journal:  Microb Cell Fact       Date:  2009-06-05       Impact factor: 5.328

Review 6.  Side effects of chaperone gene co-expression in recombinant protein production.

Authors:  Mónica Martínez-Alonso; Elena García-Fruitós; Neus Ferrer-Miralles; Ursula Rinas; Antonio Villaverde
Journal:  Microb Cell Fact       Date:  2010-09-02       Impact factor: 5.328

7.  Comparison of two codon optimization strategies to enhance recombinant protein production in Escherichia coli.

Authors:  Hugo G Menzella
Journal:  Microb Cell Fact       Date:  2011-03-03       Impact factor: 5.328

8.  Recombinant protein quality evaluation: proposal for a minimal information standard.

Authors:  Ashley M Buckle; Mark A Bate; Steve Androulakis; Mario Cinquanta; Jerome Basquin; Fabien Bonneau; Deb K Chatterjee; Davide Cittaro; Susanne Gräslund; Alicja Gruszka; Rebecca Page; Sabine Suppmann; Jun X Wheeler; Deborah Agostini; Mike Taussig; Chris F Taylor; Stephen P Bottomley; Antonio Villaverde; Ario de Marco
Journal:  Stand Genomic Sci       Date:  2011-11-22

9.  Intracellular CXCR4⁺ cell targeting with T22-empowered protein-only nanoparticles.

Authors:  Ugutz Unzueta; María Virtudes Céspedes; Neus Ferrer-Miralles; Isolda Casanova; Juan Cedano; José Luis Corchero; Joan Domingo-Espín; Antonio Villaverde; Ramón Mangues; Esther Vázquez
Journal:  Int J Nanomedicine       Date:  2012-08-15

10.  Learning about protein solubility from bacterial inclusion bodies.

Authors:  Mónica Martínez-Alonso; Nuria González-Montalbán; Elena García-Fruitós; Antonio Villaverde
Journal:  Microb Cell Fact       Date:  2009-01-08       Impact factor: 5.328

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