Identification of the cognate response regulator of the orphan histidine kinase OhkA involved in both secondary metabolism and morphological differentiation in Streptomyces coelicolor

2021 ◽  
Author(s):  
Guosong Zheng ◽  
Panpan Liu ◽  
Wenyan He ◽  
Hengnuo Tao ◽  
Zhen Yang ◽  
...  
Keyword(s):  
Secondary Metabolism ◽  
Histidine Kinase ◽  
Response Regulator ◽  
Streptomyces Coelicolor ◽  
Morphological Differentiation ◽  
Cognate Response Regulator

scholarly journals The Level of AdpA Directly Affects Expression of Developmental Genes in Streptomyces coelicolor

2011 ◽  
Vol 193 (22) ◽  
pp. 6358-6365 ◽  
Author(s):  
Marcin Wolański ◽  
Rafał Donczew ◽  
Agnieszka Kois-Ostrowska ◽  
Paweł Masiewicz ◽  
Dagmara Jakimowicz ◽  
...  
Keyword(s):  
Early Stage ◽  
Response Regulator ◽  
Streptomyces Coelicolor ◽  
Streptomyces Griseus ◽  
Morphological Differentiation ◽  
Aerial Mycelium ◽  
Content Type ◽  
Protein Functions

AdpA is a key regulator of morphological differentiation inStreptomyces. In contrast toStreptomyces griseus, relatively little is known about AdpA protein functions inStreptomyces coelicolor. Here, we report for the first time the translation accumulation profile of theS. coelicoloradpA(adpASc) gene; the level ofS. coelicolorAdpA (AdpASc) increased, reaching a maximum in the early stage of aerial mycelium formation (after 36 h), and remained relatively stable for the next several hours (48 to 60 h), and then the signal intensity decreased considerably. AdpAScspecifically binds theadpAScpromoter regionin vitroandin vivo, suggesting that its expression is autoregulated; surprisingly, in contrast toS. griseus, the protein presumably acts as a transcriptional activator. We also demonstrate a direct influence of AdpAScon the expression of several genes whose products play key roles in the differentiation ofS. coelicolor: STI, a protease inhibitor; RamR, an atypical response regulator that itself activates expression of the genes for a small modified peptide that is required for aerial growth; and ClpP1, an ATP-dependent protease. The diverse influence of AdpAScprotein on the expression of the analyzed genes presumably results mainly from different affinities of AdpAScprotein to individual promoters.

scholarly journals Biochemical Activities of the absA Two-Component System of Streptomyces coelicolor

2005 ◽  
Vol 187 (2) ◽  
pp. 687-696 ◽  
Author(s):  
Nancy L. Sheeler ◽  
Susan V. MacMillan ◽  
Justin R. Nodwell
Keyword(s):  
Transcriptional Repression ◽  
Kinase Activity ◽  
Response Regulator ◽  
Streptomyces Coelicolor ◽  
Point Mutations ◽  
Stable State ◽  
Sensor Kinase ◽  
Two Component System ◽  
Antibiotic Synthesis ◽  
Cognate Response Regulator

ABSTRACT The AbsA1 sensor kinase and its cognate response regulator AbsA2 are important regulators of antibiotic synthesis in Streptomyces coelicolor. While certain point mutations in absA1 reduce or eliminate the synthesis of several antibiotics, null mutations in these genes bring about enhanced antibiotic synthesis. We show here that AbsA1, which is unusual in sequence and structure, is both an AbsA2 kinase and an AbsA2∼P phosphatase. The half-life of AbsA2∼P in solution is 68.6 min, consistent with a role in maintaining a relatively stable state of transcriptional repression or activation. We find that mutations in the absA locus that enhance antibiotic synthesis impair AbsA2 kinase activity and that mutations that repress antibiotic synthesis impair AbsA2∼P phosphatase activity. These results support a model in which the phosphorylation state of AbsA2 is determined by the balance of the kinase and phosphatase activities of AbsA1 and where AbsA2∼P represses antibiotic biosynthetic genes either directly or indirectly.

scholarly journals The RNA Polymerase Omega Factor RpoZ Is Regulated by PhoP and Has an Important Role in Antibiotic Biosynthesis and Morphological Differentiation in Streptomyces coelicolor

2011 ◽  
Vol 77 (21) ◽  
pp. 7586-7594 ◽  
Author(s):  
Fernando Santos-Beneit ◽  
Mónica Barriuso-Iglesias ◽  
Lorena T. Fernández-Martínez ◽  
Miriam Martínez-Castro ◽  
Alberto Sola-Landa ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Response Regulator ◽  
Antibiotic Production ◽  
Streptomyces Coelicolor ◽  
Morphological Differentiation ◽  
Luciferase Reporter ◽  
Antibiotic Biosynthesis ◽  
Binding Assays ◽  
Content Type ◽  
Phosphate Depletion

ABSTRACTThe RNA polymerase (RNAP) omega factor (ω) forms a complex with the α2ββ′ core of this enzyme in bacteria. We have characterized therpoZgene ofStreptomyces coelicolor, which encodes a small protein (90 amino acids) identified as the omega factor. Deletion of therpoZgene resulted in strains with a slightly reduced growth rate, although they were still able to sporulate. The biosynthesis of actinorhodin and, particularly, that of undecylprodigiosin were drastically reduced in the ΔrpoZstrain, suggesting that expression of these secondary metabolite biosynthetic genes is dependent upon the presence of RpoZ in the RNAP complex. Complementation of the ΔrpoZmutant with the wild-typerpoZallele restored both phenotype and antibiotic production. Interestingly, therpoZgene contains a PHO box in its promoter region. DNA binding assays showed that the phosphate response regulator PhoP binds to such a region. Since luciferase reporter studies showed thatrpoZpromoter activity was increased in a ΔphoPbackground, it can be concluded thatrpoZis controlled negatively by PhoP, thus connecting phosphate depletion regulation with antibiotic production and morphological differentiation inStreptomyces.

scholarly journals The Receiver Domain of Hybrid Histidine Kinase VirA: an Enhancing Factor for vir Gene Expression in Agrobacterium tumefaciens

2010 ◽  
Vol 192 (6) ◽  
pp. 1534-1542 ◽  
Author(s):  
Arlene A. Wise ◽  
Fang Fang ◽  
Yi-Han Lin ◽  
Fanglian He ◽  
David G. Lynn ◽  
...  
Keyword(s):  
Gene Expression ◽  
Agrobacterium Tumefaciens ◽  
Histidine Kinase ◽  
Response Regulator ◽  
Multicopy Plasmid ◽  
Wild Type ◽  
Receiver Domain ◽  
Native Promoter ◽  
Cognate Response Regulator ◽  
Hybrid Histidine Kinase

ABSTRACT The plant pathogen Agrobacterium tumefaciens expresses virulence (vir) genes in response to chemical signals found at the site of a plant wound. VirA, a hybrid histidine kinase, and its cognate response regulator, VirG, regulate vir gene expression. The receiver domain at the carboxyl end of VirA has been described as an inhibitory element because its removal increased vir gene expression relative to that of full-length VirA. However, experiments that characterized the receiver region as an inhibitory element were performed in the presence of constitutively expressed virG. We show here that VirA's receiver domain is an activating factor if virG is expressed from its native promoter on the Ti plasmid. When virAΔR was expressed from a multicopy plasmid, both sugar and the phenolic inducer were essential for vir gene expression. Replacement of wild-type virA on pTi with virAΔR precluded vir gene induction, and the cells did not accumulate VirG or induce transcription of a virG-lacZ fusion in response to acetosyringone. These phenotypes were corrected if the virG copy number was increased. In addition, we show that the VirA receiver domain can interact with the VirG DNA-binding domain.

scholarly journals Intra- and intermolecular domain interactions among novel two-component system proteins coded by Rv0600c, Rv0601c and Rv0602c of Mycobacterium tuberculosis

Microbiology ◽  
2009 ◽  
Vol 155 (3) ◽  
pp. 772-779 ◽  
Author(s):  
Rashmi Shrivastava ◽  
Ananta Kumar Ghosh ◽  
Amit Kumar Das
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Histidine Kinase ◽  
Response Regulator ◽  
Dominant Role ◽  
Phosphoryl Group ◽  
Two Component System ◽  
Component System ◽  
Two Component ◽  
Domain Interactions ◽  
Cognate Response Regulator

Two-component signal transduction pathways comprising a histidine kinase and its cognate response regulator play a dominant role in the adaptation of Mycobacterium tuberculosis to its host, and its virulence, pathogenicity and latency. Autophosphorylation occurs at a conserved histidine of the histidine kinase and subsequently the phosphoryl group is transferred to the conserved aspartate of its cognate response regulator. Among the twelve two-component systems of M. tuberculosis, Rv0600c (HK1), Rv0601c (HK2) and Rv0602c (TcrA) are annotated as a unique three-protein two-component system. HK1 contains an ATP-binding domain, and HK2, a novel Hpt mono-domain protein, contains the conserved phosphorylable histidine residue. HK1 and HK2 complement each other's functions. Interactions among different domains of the HK1, HK2 and TcrA proteins were studied using a yeast two-hybrid system. Self-interaction was observed for HK2 but not for HK1 or TcrA. HK2 was found to interact reasonably well with both HK1 and TcrA, but HK1 interacted weakly with TcrA. The conserved aspartate-containing receiver domain of TcrA interacted well with HK2 but not with HK1. These results suggest the existence of a novel signalling mechanism amongst HK1–HK2–TcrA, and a model for this mechanism is proposed.

scholarly journals Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Elina Multamäki ◽  
Rahul Nanekar ◽  
Dmitry Morozov ◽  
Topias Lievonen ◽  
David Golonka ◽  
...  
Keyword(s):  
Histidine Kinase ◽  
Deinococcus Radiodurans ◽  
Response Regulator ◽  
Red Light ◽  
Kinase Domain ◽  
Structural Level ◽  
Signaling Systems ◽  
Two Component ◽  
Cognate Response Regulator ◽  
Absorbing States

AbstractBacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model bacteriophytochrome from Deinococcus radiodurans (DrBphP) lacks detectable kinase activity. Here, we resolve this long-standing conundrum by comparatively analyzing the interactions and output activities of DrBphP and a bacteriophytochrome from Agrobacterium fabrum (Agp1). Whereas Agp1 acts as a conventional histidine kinase, we identify DrBphP as a light-sensitive phosphatase. While Agp1 binds its cognate response regulator only transiently, DrBphP does so strongly, which is rationalized at the structural level. Our data pinpoint two key residues affecting the balance between kinase and phosphatase activities, which immediately bears on photoreception and two-component signaling. The opposing output activities in two highly similar bacteriophytochromes suggest the use of light-controllable histidine kinases and phosphatases for optogenetics.

Sign in / Sign up

Export Citation Format

Share Document