TY - JOUR
T1 - The mono-ADP-ribosyltransferases Alt and ModB of bacteriophage T4: Target proteins identified
AU - Depping, Reinhard
AU - Lohaus, Christiane
AU - Meyer, Helmut E.
AU - Rüger, Wolfgang
N1 - Funding Information:
The authors thank Jan Tkacz for a considerate discussion of the manuscript. We are grateful to E. Deuerling for her gift of purified E. coli trigger factor and to U. Aschke for excellent technical assistance. We gratefully acknowledge the financial support of the Deutsche Forschungsgemeinschaft by Grant RU 123-29-1.
Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2005/10/7
Y1 - 2005/10/7
N2 - Infection of Escherichia coli by bacteriophage T4 leads to the expression of three phage mono-ADP-ribosyltransferases (namely, Alt, ModA, and ModB), each of which modifies a distinct group of host proteins. To improve understanding of these interactions and their consequences for the T4 replication cycle, we used high-resolution two-dimensional gel electrophoresis and mass-spectrometry to identify some of the putative target proteins ADP-ribosylated in vitro by Alt (total ∼27) and ModB (total ∼8). E. coli trigger factor and the elongation factor EF-Tu were 2 targets of ModB action, and these proteins were among the 10 identified as targets of Alt, hinting that these factors are involved in phage replication.
AB - Infection of Escherichia coli by bacteriophage T4 leads to the expression of three phage mono-ADP-ribosyltransferases (namely, Alt, ModA, and ModB), each of which modifies a distinct group of host proteins. To improve understanding of these interactions and their consequences for the T4 replication cycle, we used high-resolution two-dimensional gel electrophoresis and mass-spectrometry to identify some of the putative target proteins ADP-ribosylated in vitro by Alt (total ∼27) and ModB (total ∼8). E. coli trigger factor and the elongation factor EF-Tu were 2 targets of ModB action, and these proteins were among the 10 identified as targets of Alt, hinting that these factors are involved in phage replication.
UR - http://www.scopus.com/inward/record.url?scp=24044441606&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2005.08.023
DO - 10.1016/j.bbrc.2005.08.023
M3 - Journal articles
C2 - 16112649
AN - SCOPUS:24044441606
SN - 0006-291X
VL - 335
SP - 1217
EP - 1223
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -
