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Prolyl isomerization as a molecular timer in phage infection

Title data

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

Official URL: Volltext

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Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 15937494
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 27 Apr 2015 07:32
Last Modified: 27 Apr 2015 07:32
URI: https://eref.uni-bayreuth.de/id/eprint/10825