TITLE:
Non-Stem Amino Acids Are Involved in the Phage P22 TSP NTD Stability
AUTHORS:
Karthikeya Venkatesan, Jeremie Williams, Robert Villafane
KEYWORDS:
N-Terminal Domain (NTD), P22 Phage, Tailspike Protein (TSP), Mutagenesis, Structural Stability
JOURNAL NAME:
Advances in Microbiology,
Vol.4 No.9,
July
24,
2014
ABSTRACT: The P22 phage
system is an intensely studied model system. Studies have ranged from biochemical
analysis of basic life processes to the use of this phage for phage therapy.
The phage tailspike protein (TSP) has itself been the subject of intensive
studies over the past fifty years. The P22 TSP is essential for initiation of
the infection process and instrumental as the last protein assembled onto the
phage particle structure to complete its assembly. It has also been the subject
for many structural studies including cryoelectron microscopic analysis and
photophysical studies. It has been a model for in vivo and in vitro protein folding including analysis using P22 TSP temperature-sensitive for
folding mutations (tsf). Recently the
structure and function of the N-terminal domain (NTD), including some aspects
of the structural stability of the P22 TSP NTD (aa1-aa108), are being
genetically dissected. This report strongly supports the notion that two amino
acids, not localized to the internal NTD dome stem, are important in the
structural stability of the P22 TSP NTD.