Literature DB >> 19562111

Engineering and exploiting protein assemblies in synthetic biology.

David Papapostolou1, Stefan Howorka.   

Abstract

Many biologically relevant structures are formed by the self-assembly of identical protein units. Examples include virus capsids or cytoskeleton components. Synthetic biology can harness these bottom-up assemblies and expand their scope for applications in cell biology and biomedicine. Nanobiotechnology and materials science also stand to gain from assemblies with unique nanoscale periodicity. In these disciplines, the soft scaffolds can serve as templates to produce new metallic or inorganic materials of predefined dimensions. This review article describes how the structure and function of biological assemblies has inspired researchers to develop engineered systems with designed properties for new biomolecular applications.

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Year:  2009        PMID: 19562111     DOI: 10.1039/b902440a

Source DB:  PubMed          Journal:  Mol Biosyst        ISSN: 1742-2051


  19 in total

1.  Short N-terminal sequences package proteins into bacterial microcompartments.

Authors:  Chenguang Fan; Shouqiang Cheng; Yu Liu; Cristina M Escobar; Christopher S Crowley; Robert E Jefferson; Todd O Yeates; Thomas A Bobik
Journal:  Proc Natl Acad Sci U S A       Date:  2010-03-22       Impact factor: 11.205

2.  Characterization of a highly flexible self-assembling protein system designed to form nanocages.

Authors:  Dustin P Patterson; Min Su; Titus M Franzmann; Aaron Sciore; Georgios Skiniotis; E Neil G Marsh
Journal:  Protein Sci       Date:  2013-12-16       Impact factor: 6.725

3.  The N-terminal region of the medium subunit (PduD) packages adenosylcobalamin-dependent diol dehydratase (PduCDE) into the Pdu microcompartment.

Authors:  Chenguang Fan; Thomas A Bobik
Journal:  J Bacteriol       Date:  2011-08-05       Impact factor: 3.490

Review 4.  Biomolecular engineering for nanobio/bionanotechnology.

Authors:  Teruyuki Nagamune
Journal:  Nano Converg       Date:  2017-04-24

5.  Flexible, symmetry-directed approach to assembling protein cages.

Authors:  Aaron Sciore; Min Su; Philipp Koldewey; Joseph D Eschweiler; Kelsey A Diffley; Brian M Linhares; Brandon T Ruotolo; James C A Bardwell; Georgios Skiniotis; E Neil G Marsh
Journal:  Proc Natl Acad Sci U S A       Date:  2016-07-18       Impact factor: 11.205

6.  The PduM protein is a structural component of the microcompartments involved in coenzyme B(12)-dependent 1,2-propanediol degradation by Salmonella enterica.

Authors:  Sharmistha Sinha; Shouqiang Cheng; Chenguang Fan; Thomas A Bobik
Journal:  J Bacteriol       Date:  2012-02-17       Impact factor: 3.490

7.  Evaluation of a symmetry-based strategy for assembling protein complexes.

Authors:  Dustin P Patterson; Ankur M Desai; Mark M Banaszak Holl; E Neil G Marsh
Journal:  RSC Adv       Date:  2011-10-21       Impact factor: 3.361

8.  Fast and easy protocol for the purification of recombinant S-layer protein for synthetic biology applications.

Authors:  Julie E Norville; Deborah F Kelly; Thomas F Knight; Angela M Belcher; Thomas Walz
Journal:  Biotechnol J       Date:  2011-06-17       Impact factor: 4.677

9.  Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments.

Authors:  Chenguang Fan; Shouqiang Cheng; Sharmistha Sinha; Thomas A Bobik
Journal:  Proc Natl Acad Sci U S A       Date:  2012-08-27       Impact factor: 11.205

10.  The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+ internally within the Pdu microcompartment of Salmonella enterica.

Authors:  Shouqiang Cheng; Chenguang Fan; Sharmistha Sinha; Thomas A Bobik
Journal:  PLoS One       Date:  2012-10-15       Impact factor: 3.240

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