title: Functional specialization in regulation and quality control in thermal adaptive evolution.
abstract: Distinctive survival strategies, specialized in regulation and in quality control, were observed in thermal adaptive evolution with a laboratory Escherichia coli strain. The two specialists carried a single mutation either within rpoH or upstream of groESL, which led to the activated global regulation by sigma factor 32 or an increased amount of GroEL/ES chaperonins, respectively. Although both specialists succeeded in thermal adaptation, the common winner of the evolution was the specialist in quality control, that is, the strategy of chaperonin-mediated protein folding. To understand this evolutionary consequence, multilevel analyses of cellular status, for example, transcriptome, protein and growth fitness, were carried out. The specialist in quality control showed less change in transcriptional reorganization responding to temperature increase, which was consistent with the finding of that the two specialists showed the biased expression of molecular chaperones. Such repressed changes in gene expression seemed to be advantageous for long-term sustainability because a specific increase in chaperonins not only facilitated the folding of essential gene products but also saved cost in gene expression compared with the overall transcriptional increase induced by rpoH regulation. Functional specialization offered two strategies for successful thermal adaptation, whereas the evolutionary advantageous was more at the points of cost-saving in gene expression and the essentiality in protein folding.
authors.affiliation: Graduate School of Information Science and Technology, Osaka University, Osaka, 565-0871, Japan.
authors.forename: Kazuma
authors.initials: K
authors.lastname: Yama
authors.affiliation: Graduate School of Life and Environmental Sciences, University of Tsukuba, Ibaraki, 305-8572, Japan.
authors.forename: Yuki
authors.initials: Y
authors.lastname: Matsumoto
authors.affiliation: Graduate School of Information Science and Technology, Osaka University, Osaka, 565-0871, Japan.
authors.forename: Yoshie
authors.initials: Y
authors.lastname: Murakami
authors.affiliation: Graduate School of Information Science and Technology, Osaka University, Osaka, 565-0871, Japan.
authors.forename: Shigeto
authors.initials: S
authors.lastname: Seno
authors.affiliation: Graduate School of Information Science and Technology, Osaka University, Osaka, 565-0871, Japan.
authors.forename: Hideo
authors.initials: H
authors.lastname: Matsuda
authors.affiliation: Research Institute for Microbial Diseases, Osaka University, Osaka, 565-0871, Japan.
authors.forename: Kazuyoshi
authors.initials: K
authors.lastname: Gotoh
authors.affiliation: Research Institute for Microbial Diseases, Osaka University, Osaka, 565-0871, Japan.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Motooka
authors.affiliation: Research Institute for Microbial Diseases, Osaka University, Osaka, 565-0871, Japan.
authors.forename: Shota
authors.initials: S
authors.lastname: Nakamura
authors.affiliation: Graduate School of Life and Environmental Sciences, University of Tsukuba, Ibaraki, 305-8572, Japan.
authors.forename: Bei-Wen
authors.initials: BW
authors.lastname: Ying
authors.affiliation: Graduate School of Information Science and Technology, Osaka University, Osaka, 565-0871, Japan.|Graduate School of Frontier Biosciences, Osaka University, Osaka, 565-0871, Japan.|Exploratory Research for Advanced Technology, Japan Science and Technology Agency, Tokyo, 102-0076, Japan.
authors.forename: Tetsuya
authors.initials: T
authors.lastname: Yomo
mesh_terms: D000220:Adaptation, Biological / Q000235:genetics*; D001426:Bacterial Proteins / Q000378:metabolism; D005075:Biological Evolution; D018834:Chaperonin 60 / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding; D012808:Sigma Factor / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D012808:Sigma Factor; C069774:heat-shock sigma factor 32