Prolyl isomerization as a molecular timer in phage infection

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Eckert, Barbara ; Martin, Andreas ; Balbach, Jochen ; Schmid, Franz X.:
Prolyl isomerization as a molecular timer in phage infection.
In: Nature Structural & Molecular Biology. Bd. 12 (2005) Heft 7 . - S. 619-623.
ISSN 1545-9985
DOI: https://doi.org/10.1038/nsmb946

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Abstract

Prolyl cis-trans isomerizations are intrinsically slow reactions and known to be rate-limiting in many protein folding reactions. Here we report that a proline is used as a molecular timer in the infection of Escherichia coli cells by the filamentous phage fd. The phage is activated for infection by the disassembly of the two N-terminal domains, N1 and N2, of its gene-3-protein, which is located at the phage tip. Pro213, in the hinge between N1 and N2, sets a timer for the infective state. The timer is switched on by cis-to-trans and switched off by the unusually slow trans-to-cis isomerization of the Gln212-Pro213 peptide bond. The switching rate and thus the infectivity of the phage are determined by the local sequence around Pro213, and can be tuned by mutagenesis.