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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004458naa a2200505 4500
001oai:research.chalmers.se:abf4ba77-8b02-4d1d-a408-9bb1b7432542
003SwePub
008171007s2014 | |||||||||||000 ||eng|
0247 a https://research.chalmers.se/publication/2002022 URI
0247 a https://doi.org/10.1093/gbe/evu0562 DOI
040 a (SwePub)cth
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
1001 a Shi, Lei,d 1981u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)slei
2451 0a Evolution of Bacterial Protein-Tyrosine Kinases and Their Relaxed Specificity Toward Substrates
264 c 2014-04-11
264 1b Oxford University Press (OUP),c 2014
338 a electronic2 rdacarrier
520 a It has often been speculated that bacterial protein-tyrosine kinases (BY-kinases) evolve rapidly and maintain relaxed substrate specificity to quickly adopt new substrates when evolutionary pressure in that direction arises. Here, we report a phylogenomic and biochemical analysis of BY-kinases, and their relationship to substrates aimed to validate this hypothesis. Our results suggest that BY-kinases are ubiquitously distributed in bacterial phyla and underwent a complex evolutionary history, affected considerably by gene duplications and horizontal gene transfer events. This is consistent with the fact that the BY-kinase sequences represent a high level of substitution saturation and have a higher evolutionary rate compared with other bacterial genes. On the basis of similarity networks, we could classify BY kinases into three main groups with 14 subgroups. Extensive sequence conservation was observed only around the three canonical Walker motifs, whereas unique signatures proposed the functional speciation and diversification within some subgroups. The relationship between BY-kinases and their substrates was analyzed using a ubiquitous substrate (Ugd) and some Firmicute-specific substrates (YvyG and YjoA) from Bacillus subtilis. No evidence of coevolution between kinases and substrates at the sequence level was found. Seven BY-kinases, including well-characterized and previously uncharacterized ones, were used for experimental studies. Most of the tested kinases were able to phosphorylate substrates from B. subtilis (Ugd, YvyG, and YjoA), despite originating from very distant bacteria. Our results are consistent with the hypothesis that BY-kinases have evolved relaxed substrate specificity and are probably maintained as rapidly evolving platforms for adopting new substrates.
650 7a NATURVETENSKAPx Biologix Bioinformatik och systembiologi0 (SwePub)106102 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Bioinformatics and Systems Biology0 (SwePub)106102 hsv//eng
653 a kinase-substrate coevolution
653 a phylogeny
653 a bacterial protein kinases
653 a BY-kinases
653 a kinase evolution
653 a kinase classification
7001 a Ji, Boyang,d 1983u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)bojand
7001 a Kolar-Znika, L.u Sveučilište u Zagrebu,University of Zagreb,INRA Centre de Recherche de Versailles-Grignon4 aut
7001 a Boskovic, A.u INRA Centre de Recherche de Versailles-Grignon,Sveučilište u Zagrebu,University of Zagreb4 aut
7001 a Jadeau, F.u Université de Lyon4 aut
7001 a Combet, C.u Université de Lyon4 aut
7001 a Grangeasse, C.u Université de Lyon4 aut
7001 a Franjevic, D.u Sveučilište u Zagrebu,University of Zagreb4 aut
7001 a Talla, E.u Aix-Marseille Université,Aix Marseille University4 aut
7001 a Mijakovic, Ivan,d 1975u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)ivanmi
7102 a Chalmers tekniska högskolab Sveučilište u Zagrebu4 org
7730 t Genome Biology and Evolutiond : Oxford University Press (OUP)g 6:4, s. 800-817q 6:4<800-817x 1759-6653
8564 u http://dx.doi.org/10.1093/gbe/evu056y FULLTEXT
8564 u https://research.chalmers.se/publication/200202/file/200202_Fulltext.pdfx primaryx freey FULLTEXT
8564 u https://academic.oup.com/gbe/article-pdf/6/4/800/17922418/evu056.pdf
8564 8u https://research.chalmers.se/publication/200202
8564 8u https://doi.org/10.1093/gbe/evu056

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