The Library
Split histidine kinases enable ultrasensitivity and bistability in two-component signaling networks
Tools
Amin, Munia, Porter, Steven L. and Soyer, Orkun S. (2013) Split histidine kinases enable ultrasensitivity and bistability in two-component signaling networks. PLoS Computational Biology, Volume 9 (Number 3). Article no. e1002949. doi:10.1371/journal.pcbi.1002949 ISSN 1553-7358.
|
Text
WRAP_Soyer_journal.pcbi.1002949.pdf - Published Version Available under License Creative Commons Attribution Non-commercial. Download (1004Kb) | Preview |
Official URL: http://dx.doi.org/10.1371/journal.pcbi.1002949
Abstract
Bacteria sense and respond to their environment through signaling cascades generally referred to as two-component signaling networks. These networks comprise histidine kinases and their cognate response regulators. Histidine kinases have a number of biochemical activities: ATP binding, autophosphorylation, the ability to act as a phosphodonor for their response regulators, and in many cases the ability to catalyze the hydrolytic dephosphorylation of their response regulator. Here, we explore the functional role of “split kinases” where the ATP binding and phosphotransfer activities of a conventional histidine kinase are split onto two distinct proteins that form a complex. We find that this unusual configuration can enable ultrasensitivity and bistability in the signal-response relationship of the resulting system. These dynamics are displayed under a wide parameter range but only when specific biochemical requirements are met. We experimentally show that one of these requirements, namely segregation of the phosphatase activity predominantly onto the free form of one of the proteins making up the split kinase, is met in Rhodobacter sphaeroides. These findings indicate split kinases as a bacterial alternative for enabling ultrasensitivity and bistability in signaling networks. Genomic analyses reveal that up 1.7% of all identified histidine kinases have the potential to be split and bifunctional.
Item Type: | Journal Article | ||||
---|---|---|---|---|---|
Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Library of Congress Subject Headings (LCSH): | Biochemistry, Amino acids -- Analysis, Genomics -- Analysis | ||||
Journal or Publication Title: | PLoS Computational Biology | ||||
Publisher: | Public Library of Science | ||||
ISSN: | 1553-7358 | ||||
Official Date: | 2013 | ||||
Dates: |
|
||||
Volume: | Volume 9 | ||||
Number: | Number 3 | ||||
Page Range: | Article no. e1002949 | ||||
DOI: | 10.1371/journal.pcbi.1002949 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Open Access (Creative Commons) | ||||
Date of first compliant deposit: | 24 December 2015 | ||||
Date of first compliant Open Access: | 24 December 2015 |
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |
Downloads
Downloads per month over past year