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Heterodimer formation within universal stress protein classes revealed by an in silico and experimental approach.

Artikel i vetenskaplig tidskrift
Författare Laurence Nachin
Lars Brive
Cecilia Persson
Peder Svensson
Thomas Nyström
Publicerad i Journal of molecular biology
Volym 380
Nummer/häfte 2
Sidor 340-50
ISSN 1089-8638
Publiceringsår 2008
Publicerad vid Institutionen för cell- och molekylärbiologi
Svenskt NMR-centrum vid Göteborgs universitet
Sidor 340-50
Språk en
Länkar dx.doi.org/10.1016/j.jmb.2008.04.07...
Ämnesord Amino Acid Sequence, Dimerization, Escherichia coli Proteins, chemistry, classification, genetics, Heat-Shock Proteins, chemistry, classification, genetics, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Structure, Quaternary, Sequence Analysis, Protein, Two-Hybrid System Techniques
Ämneskategorier Strukturbiologi, Molekylärbiologi, Cellbiologi, Mikrobiologi, Bioinformatik och systembiologi

Sammanfattning

Universal stress proteins (Usps) are found in all kingdoms of life and can be divided into four classes by phylogenic analysis. According to available structures, Usps exist as homodimers, and genetic studies show that their cellular assignments are extensive, including functions relating to stress resistance, carbon metabolism, cellular adhesion, motility, and bacterial virulence. We approached the question of how Usps can achieve such a variety of functions in a cell by using a new procedure for statistical analysis of multiple sequence alignments, based on physicochemically related values for each amino acid residue of Usp dimer interfaces. The results predicted that Usp proteins within a class may, in addition to forming homodimers, be able to form heterodimers. Using Escherichia coli Usps as model proteins, we confirmed the existence of such interactions. We especially focused on class I UspA and UspC and demonstrated that they are able to form homo- and heterodimers in vitro and in vivo. We suggest that this ability to form both homo- and heterodimers may allow for an expansion of the functional repertoire of Usps and explains why organisms usually contain multiple usp paralogues.

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