Evolution and tinkering: what do a protein kinase, a transcriptional regulator and chromosome segregation/cell division proteins have in common?
Journal article, 2016

In this study, we focus on functional interactions among multi-domain proteins which share a common evolutionary origin. The examples we develop are four Bacillus subtilis proteins, which all possess an ATP-binding Walker motif: the bacterial tyrosine kinase (BY-kinase) PtkA, the chromosome segregation protein Soj (ParA), the cell division protein MinD and a transcription regulator SalA. These proteins have arisen via duplication of the ancestral ATP-binding domain, which has undergone fusions with other functional domains in the process of divergent evolution. We point out that these four proteins, despite having very different physiological roles, engage in an unusually high number of binary functional interactions. Namely, MinD attracts Soj and PtkA to the cell pole, and in addition, activates the kinase function of PtkA. SalA also activates the kinase function of PtkA, and it gets phosphorylated by PtkA as well. The consequence of this phosphorylation is the activation of SalA as a transcriptional repressor. We hypothesize that these functional interactions remain preserved during divergent evolution and represent a constraint on the process of evolutionary "tinkering", brought about by fusions of different functional domains.

Transcriptional regulation

DNA-binding domain

Cell division

ATPase

Protein phosphorylation

Author

Abderahmane Derouiche

Chalmers, Biology and Biological Engineering, Systems and Synthetic Biology

Lei Shi

Chalmers, Biology and Biological Engineering, Systems and Synthetic Biology

Aida Kalantari

Chalmers, Biology and Biological Engineering, Systems and Synthetic Biology

Ivan Mijakovic

Chalmers, Biology and Biological Engineering, Systems and Synthetic Biology

Current Genetics

0172-8083 (ISSN) 1432-0983 (eISSN)

Vol. 62 1 67-70

Subject Categories

Biochemistry and Molecular Biology

DOI

10.1007/s00294-015-0513-y

More information

Created

10/7/2017