Prof. Dr. E. Bornberg-Bauer
Modular evolution of proteins
The prediction of function for a given protein sequence by comparative and evolutionary analysis is a well established principle. Due to the low conservation of
many sequence regions and the modular rearrangements of proteins it is often useful to break down the problem and view proteins as strings of functional units. These
domains (or, at the sequence level, motifs) are more conserved during evolution and constitute the basic elements of modular evolution within and in
between organisms, e.g, by lateral gene-transfer. Other events which can be more easily traced by viewing proteins as strings of domains rather than as strings of
amino-acids are circular permutations . They represent non-linear arrangements of domains such that they can not be detected using the standard sequence
alignment procedures.
Most proteins consist of two or more domains, giving rise to a variety of combinations of domain arrangements. Another level of complexity arises because proteins
themselves can form complexes with small molecules, nucleic acids or other proteins. The networks of both domain combinations and protein interactions can be
conceptualised as graphs and these graphs can be analysed conveniently by computational methods. We are
working both on large scale projects to study the promiscuity of domains in general but also specialise on transcription factors and improved methods for their prediction
by sequence analysis. Theoretical studies on how recombination influences the adaptation and evolve-ability of protein domains complement the sequence based
studies. This research leads to an understanding of molecular evolution and eventually results in improved and specialised algorithms for genome analysis.
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