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

    Tutkimustuotos: ArtikkeliScientificvertaisarvioitu

    Abstrakti

    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.

    AlkuperäiskieliEnglanti
    Sivut225-233
    Sivumäärä9
    JulkaisuVIROLOGY
    Vuosikerta482
    DOI - pysyväislinkit
    TilaJulkaistu - 2015
    OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä

    Tutkimusalat

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

    Julkaisufoorumi-taso

    • Jufo-taso 1

    Sormenjälki

    Sukella tutkimusaiheisiin 'Non-structural proteins P17 and P33 are involved in the assembly of the internal membrane-containing virus PRD1'. Ne muodostavat yhdessä ainutlaatuisen sormenjäljen.

    Siteeraa tätä