title: Binase-like guanyl-preferring ribonucleases are new members of Bacillus PhoP regulon.
abstract: 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.
authors.affiliation: Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, United Kingdom; Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, 420008, Russian Federation. Electronic address: ulyanova.vera@gmail.com.
authors.forename: Vera
authors.initials: V
authors.lastname: Ulyanova
authors.affiliation: Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, 420008, Russian Federation. Electronic address: valentina.vershinina@kpfu.ru.
authors.forename: Valentina
authors.initials: V
authors.lastname: Vershinina
authors.affiliation: Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, 420008, Russian Federation. Electronic address: ilinskaya_kfu@mail.ru.
authors.forename: Olga
authors.initials: O
authors.lastname: Ilinskaya
authors.affiliation: Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, United Kingdom. Electronic address: colin.harwood@ncl.ac.uk.
authors.forename: Colin R
authors.initials: CR
authors.lastname: Harwood
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D015964:Gene Expression Regulation, Bacterial; D008969:Molecular Sequence Data; D059372:Nucleotide Motifs; D010802:Phylogeny; D056510:Position-Specific Scoring Matrices; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D018085:Regulon / Q000235:genetics*; D006163:Ribonuclease T1 / Q000737:chemistry / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; C061064:PhoP protein, Bacteria; D006163:Ribonuclease T1
keywords: Bacillus; Binase; Extracellular ribonuclease; Phosphate starvation; Stress response