Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli.

Autor: Karttunen J; Centre of Excellence in Biological Interactions, Department of Biological and Environmental Science and Nanoscience Center, P.O. Box 35, 40014 University of Jyväskylä, Finland., Mäntynen S; Centre of Excellence in Biological Interactions, Department of Biological and Environmental Science and Nanoscience Center, P.O. Box 35, 40014 University of Jyväskylä, Finland., Ihalainen TO; Nanoscience Center, Department of Biological and Environmental Science, P.O. Box 35, 40014 University of Jyväskylä, Finland., Lehtivuori H; Nanoscience Center, Department of Biological and Environmental Science, P.O. Box 35, 40014 University of Jyväskylä, Finland., Tkachenko NV; Department of Chemistry and Bioengineering, Tampere University of Technology, P.O. Box 541, 33101 Tampere, Finland., Vihinen-Ranta M; Nanoscience Center, Department of Biological and Environmental Science, P.O. Box 35, 40014 University of Jyväskylä, Finland., Ihalainen JA; Nanoscience Center, Department of Biological and Environmental Science, P.O. Box 35, 40014 University of Jyväskylä, Finland., Bamford JK; Centre of Excellence in Biological Interactions, Department of Biological and Environmental Science and Nanoscience Center, P.O. Box 35, 40014 University of Jyväskylä, Finland., Oksanen HM; Institute of Biotechnology and Department of Biosciences, P.O. Box 56, 00014 University of Helsinki, Finland. Electronic address: hanna.oksanen@helsinki.fi.
Jazyk: angličtina
Zdroj: Virus research [Virus Res] 2014 Jan 22; Vol. 179, pp. 44-52. Date of Electronic Publication: 2013 Nov 28.
DOI: 10.1016/j.virusres.2013.11.015
Abstrakt: Bacteria possess an intricate internal organization resembling that of the eukaryotes. The complexity is especially prominent at the bacterial cell poles, which are also known to be the preferable sites for some bacteriophages to infect. Bacteriophage PRD1 is a well-known model serving as an ideal system to study structures and functions of icosahedral internal membrane-containing viruses. Our aim was to analyze the localization and interactions of individual PRD1 proteins in its native host Escherichia coli. This was accomplished by constructing a vector library for production of fluorescent fusion proteins. Analysis of solubility and multimericity of the fusion proteins, as well as their localization in living cells by confocal microscopy, indicated that multimeric PRD1 proteins were prone to localize in the cell poles. Furthermore, PRD1 spike complex proteins P5 and P31, as fusion proteins, were shown to be functional in the virion assembly. In addition, they were shown to co-localize in the specific polar area of the cells, which might have a role in the multimerization and formation of viral protein complexes.
(Copyright © 2013 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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