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Binase-like guanyl-preferring ribonucleases are new members of Bacillus PhoP regulon

Lookup NU author(s): Vera Ulyanova, Professor Colin Harwood


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Extracellular low-molecular weight guanyl-preferring ribonucleases (LMW RNases) of Bacillus sp. comprise a group of hydrolytic enzymes that share highly similar structural and catalytic characteristics with barnase, a ribonuclease from Bacillus amyloliquefaciens, and binase, a ribonuclease from Bacillus intermedius. Although the physical-chemical and catalytic properties of Bacillus guanyl-preferring ribonucleases are very similar, there is considerably more variation in the environmental conditions that lead to the induction of the genes encoding these RNases. Based on structural differences of their genes the guanyl-preferring ribonucleases have been sub-divided into binase-like and barnase-like groups. Here we show the ability of the key regulator of phosphate deficiency response, PhoP, to direct the transcription of the binase-like RNases but not barnase-like RNases. These results, together with our demonstration that binase-like RNases are induced in response to phosphate starvation, allow us to categorise this group of ribonucleases as new members of Bacillus PhoP regulon. In contrast, the barnase-like ribonucleases are relatively insensitive to the phosphate concentration and the environmental conditions that are responsible for their induction, and the regulatory elements involved, are currently unknown. (C) 2014 Elsevier GmbH. All rights reserved.

Publication metadata

Author(s): Ulyanova V, Vershinina V, Ilinskaya O, Harwood CR

Publication type: Article

Publication status: Published

Journal: Microbiological Research

Year: 2015

Volume: 170

Pages: 131-138

Print publication date: 01/01/2015

Online publication date: 29/08/2014

Acceptance date: 24/08/2014

ISSN (print): 0944-5013

ISSN (electronic): 1618-0623

Publisher: Elsevier GmbH - Urban und Fischer


DOI: 10.1016/j.micres.2014.08.005


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Funder referenceFunder name
UNESCO-IUMS-SGM Travel Fellowship
14-14-00522Russian Research Foundation