IMP Research Report 2002

Figure 1: Eco1p - an acetyltransferase in cohesion. The image is an
artist’s view of how our understanding of protein structure and
function is emerging from a sequence alignment. It shows the joint
multiple alignment of Eco1 sequences from different organisms and
sequences of members of the GNAT superfamily of acetyltransferases.
The alignment was obtained based on domain fragment
searches, secondary structure predictions and physico-chemical
similarity of amino acid types. The three-dimensional structure of
GCN5 histone N-acetyltransferase from Tetrahymena thermophilum
[Rojas et al. Nature 1999; 401:93-98] is shown above. The
secondary structure elements of the most conserved motifs D, A,
and B that were predicted in Eco1 are colored. Eco1 is a protein
that has been previously implicated in the establishment of bridges
between sister chromatids during DNA replication. The unexpected
acetyltransferase activity of Eco1 is reported in the paper by D.
Ivanov et al. (Curr Biol. 2002, 12(4):323-328).
Figure 2: The N-terminal N-myristoylation of proteins. Myristoyl-
CoA: protein N-myristoyltransferase (NMT) recognizes the N-termini
of various eukaryotic and viral proteins and attaches myristate as
lipid anchor to direct them to diverse membranes. We refined the
sequence requirements for substrate recognition and described the
motif also in terms of characteristic deviations of physical properties
from random proteins (SWISSPROT average). Transforming our
knowledge into a scoring function, we were able to build a predictor
for this lipid modification whose selectivity and sensitivity allows
proteome-wide database annotations.
determined by interaction with experimental life
sciences. Our methodical research has been grouped
around two main lines:
1. Recognition of posttranslational modification signals
in protein sequences. We have developed a
myristoylation predictor (Figure 2).
2. Integration of diverse sequence analysis methods in
account the requirements caused by various scientific
activities, a heterogeneous network of Apple Macintosh
computers, Windows-based PCs and Unix machines
is supported.
Contact:
Frank.Eisenhaber@imp.univie.ac.at
a higher order shell (“automatic sequence analyzer”)
for applications in large-scale protein sequence
annotation; a common project with Boehringer-
Ingelheim Austria.
Computer usage and networking at the IMP
Modern experimental biological research as well as
efficient administration and maintenance of the institute
is impossible without powerful computer and network
services including Internet connections. Following the
wishes of different IMP researchers and taking into
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