title: Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli.
abstract: 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.
authors.affiliation: Centre of Excellence in Biological Interactions, Department of Biological and Environmental Science and Nanoscience Center, P.O. Box 35, 40014 University of Jyväskylä, Finland.
authors.forename: Jenni
authors.initials: J
authors.lastname: Karttunen
authors.affiliation: Centre of Excellence in Biological Interactions, Department of Biological and Environmental Science and Nanoscience Center, P.O. Box 35, 40014 University of Jyväskylä, Finland.
authors.forename: Sari
authors.initials: S
authors.lastname: Mäntynen
authors.affiliation: Nanoscience Center, Department of Biological and Environmental Science, P.O. Box 35, 40014 University of Jyväskylä, Finland.
authors.forename: Teemu O
authors.initials: TO
authors.lastname: Ihalainen
authors.affiliation: Nanoscience Center, Department of Biological and Environmental Science, P.O. Box 35, 40014 University of Jyväskylä, Finland.
authors.forename: Heli
authors.initials: H
authors.lastname: Lehtivuori
authors.affiliation: Department of Chemistry and Bioengineering, Tampere University of Technology, P.O. Box 541, 33101 Tampere, Finland.
authors.forename: Nikolai V
authors.initials: NV
authors.lastname: Tkachenko
authors.affiliation: Nanoscience Center, Department of Biological and Environmental Science, P.O. Box 35, 40014 University of Jyväskylä, Finland.
authors.forename: Maija
authors.initials: M
authors.lastname: Vihinen-Ranta
authors.affiliation: Nanoscience Center, Department of Biological and Environmental Science, P.O. Box 35, 40014 University of Jyväskylä, Finland.
authors.forename: Janne A
authors.initials: JA
authors.lastname: Ihalainen
authors.affiliation: Centre of Excellence in Biological Interactions, Department of Biological and Environmental Science and Nanoscience Center, P.O. Box 35, 40014 University of Jyväskylä, Finland.
authors.forename: Jaana K H
authors.initials: JK
authors.lastname: Bamford
authors.affiliation: Institute of Biotechnology and Department of Biosciences, P.O. Box 56, 00014 University of Helsinki, Finland. Electronic address: hanna.oksanen@helsinki.fi.
authors.forename: Hanna M
authors.initials: HM
authors.lastname: Oksanen
mesh_terms: D025622:Bacteriophage PRD1 / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000821:virology*; D042541:Intracellular Space / Q000821:virology*; D021381:Protein Transport; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D014764:Viral Proteins
keywords: Bacteria; Confocal microscopy; Membrane virus; Protein interactions; Virus assembly