Non-structural proteins P17 and P33 are involved in the assembly of the internal membrane-containing virus PRD1

Jenni Karttunen, Sari Mäntynen, Teemu O. Ihalainen, Jaana K H Bamford, Hanna M. Oksanen

    Research output: Contribution to journalArticleScientificpeer-review


    Bacteriophage PRD1, which has been studied intensively at the structural and functional levels, still has some gene products with unknown functions and certain aspects of the PRD1 assembly process have remained unsolved. In this study, we demonstrate that the phage-encoded non-structural proteins P17 and P33, either individually or together, complement the defect in a temperature-sensitive GroES mutant of Escherichia coli for host growth and PRD1 propagation. Confocal microscopy of fluorescent fusion proteins revealed co-localisation between P33 and P17 as well as between P33 and the host chaperonin GroEL. A fluorescence recovery after photobleaching assay demonstrated that the diffusion of the P33 fluorescent fusion protein was substantially slower in E. coli than theoretically calculated, presumably resulting from intermolecular interactions. Our results indicate that P33 and P17 function in procapsid assembly, possibly in association with the host chaperonin complex GroEL/GroES.

    Original languageEnglish
    Pages (from-to)225-233
    Number of pages9
    Publication statusPublished - 2015
    Publication typeA1 Journal article-refereed


    • Assembly
    • Bacteriophage
    • Chaperonin
    • Fluorescence recovery after photobleaching
    • Fluorescent protein
    • Membrane virus
    • Protein localisation

    Publication forum classification

    • Publication forum level 1


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