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Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment.
Sinha, Sharmistha; Cheng, Shouqiang; Sung, Yea Won; McNamara, Dan E; Sawaya, Michael R; Yeates, Todd O; Bobik, Thomas A.
Afiliação
  • Sinha S; Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
  • Cheng S; Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
  • Sung YW; Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
  • McNamara DE; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Sawaya MR; Department of Energy Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Yeates TO; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA; Department of Energy Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA 90095, USA; Molecular Biology Institute, University of California, Los Angel
  • Bobik TA; Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA. Electronic address: bobik@iastate.edu.
J Mol Biol ; 426(12): 2328-45, 2014 Jun 12.
Article em En | MEDLINE | ID: mdl-24747050
ABSTRACT
Bacterial microcompartments (MCPs) are the simplest organelles known. They function to enhance metabolic pathways by confining several related enzymes inside an all-protein envelope called the shell. In this study, we investigated the factors that govern MCP assembly by performing scanning mutagenesis on the surface residues of PduA, a major shell protein of the MCP used for 1,2-propanediol degradation. Biochemical, genetic, and structural analysis of 20 mutants allowed us to determine that PduA K26, N29, and R79 are crucial residues that stabilize the shell of the 1,2-propanediol MCP. In addition, we identify two PduA mutants (K37A and K55A) that impair MCP function most likely by altering the permeability of its protein shell. These are the first studies to examine the phenotypic effects of shell protein structural mutations in an MCP system. The findings reported here may be applicable to engineering protein containers with improved stability for biotechnology applications.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Salmonella typhimurium / Proteínas de Bactérias / Multimerização Proteica Tipo de estudo: Prognostic_studies Idioma: En Revista: J Mol Biol Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Estados Unidos
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Salmonella typhimurium / Proteínas de Bactérias / Multimerização Proteica Tipo de estudo: Prognostic_studies Idioma: En Revista: J Mol Biol Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Estados Unidos