A gene cluster involved in aerial mycelium formation in Streptomyces griseus encodes proteins similar to the response regulators of two-component regulatory systems and membrane translocators

Uéda, Kenji; Miyake, Katsuhide; Horinouchi, Sueharu; Beppu, Teruhiko

doi:10.1128/jb.175.7.2006-2016.1993

Cited by 69 publications

(66 citation statements)

References 46 publications

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“…Plasmid pIJ922 (carrying thiostrepton resistance) has a copy number of 1 to 2 (Hopwood et al, 1985). pSL1 used for genetic complementation of an amfR mutant was described previously (Ueda et al, 1993). S. griseus strains were grown in Bennett's\glucose [containing (g l − ") : yeast extract (Difco), 1 ; meat extract (Kyokuto), 1 ; NZ amine (Wako), 2 ; glucose (Kokusan), 10 ; pH 7n2], YMP\ glucose [containing (g l − ") : yeast extract (Difco), 2 ; meat extract (Kyokuto), 2 ; Bacto Peptone (Difco), 4 ; NaCl, 5 ; MgSO % .7H # O, 2 ; glucose (Kokusan), 10 ; pH 7n2] and nutrient broth (Difco).…”

Section: Methodsmentioning

confidence: 99%

A novel extracytoplasmic phenol oxidase of Streptomyces: its possible involvement in the onset of morphogenesis The DDBJ accession number for the sequence reported in this paper is AB056583.

et al. 2002

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Exogenous addition of copper stimulates cellular differentiation inStreptomyces spp. Several lines of evidence suggested a parallel correlation between the stimulatory effect of copper and phenol-oxidizing enzyme activities in Streptomyces griseus. Here a novel extracytoplasmic phenol oxidase (EpoA) associated with cellular development of this organism was identified and characterized. EpoA activity, examined by an in-gel stain procedure with N,N'-dimethyl-p-phenylenediamine sulfate as a substrate, was repressed by glucose and induced by copper supplied in the medium. The enzyme activity was abolished and markedly reduced in the mutants for A-factor biosynthesis and amfR, respectively, which suggested that the activity of the enzyme depends on those essential regulators for morphogenesis in S. griseus. EpoA protein was purified to homogeneity and the N-terminal amino acid sequence was determined. A homologous sequence identified in the genomic database of Streptomyces coelicolorA3(2) was used as a probe to clone the complete epoA gene of S. griseus. The deduced amino acid sequence of EpoA revealed that the mature protein with a molecular mass of 34 kDa was preceded by a signal peptide consisting of 34 aa, consistent with EpoA being a secreted enzyme. EpoA was predicted to be a laccase-type oxidase by not only the sequence similarity, but its substrate selectivity, oxidizing not tyrosine but dihydroxyphenylalanine (DOPA) to generate melanin pigment. Introduction of epoA on a plasmid partially restored both the EpoA activity and aerial mycelium productivity in an A-factor-deficient mutant. Exogenous supplementation of a substance synthesized by purified EpoA from DOPA stimulated cellular differentiation in S. griseus and several other species. Ultrafiltration indicated that the molecular mass of the putative stimulant synthesized by EpoA is between 500 and 1000 Da.

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Section: Methodsmentioning

confidence: 99%

A novel extracytoplasmic phenol oxidase of Streptomyces: its possible involvement in the onset of morphogenesis The DDBJ accession number for the sequence reported in this paper is AB056583.

et al. 2002

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“…10,11) Hence, phosphate deficiency after onset of aerial hyphae suggests, that lipoamino acids support protein cross-linking by TGase in the cell wall of S. mobaraensis. 12,13) A dispase inactivating protein (DAIP) has been characterized that can act as an additional intrinsic TGase substrate via exposed glutamine and lysine residues. Like SSTI, glutamine reactivity was lost during submerged (artificial) culture of S. mobaraensis, resulting in the formation of glutamic/lysine residue y To whom correspondence should be addressed.…”

Section: -7)mentioning

confidence: 99%

A Novel Transglutaminase Substrate fromStreptomyces mobaraensisTriggers Autolysis of Neutral Metalloproteases

Sarafeddinov¹,

Adolf²,

Mainusch³

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…Recent studies show that protein O-phosphorylation is a widespread phenomenon in streptomycetes (Umeyama et al, 2002;Horinouchi, 2003). One well-studied example is the afsK-afsR system from Streptomyces griseus (Ueda et al, 1993). The afsK and afsR genes encode a serine/ threonine PK and its targeted protein, respectively.…”

Section: Introductionmentioning

confidence: 99%

Comparative analysis of eukaryotic-type protein phosphatases in two streptomycete genomes

Shi

Zhang

2004

Microbiology

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Inspection of the genomes of Streptomyces coelicolor A3(2) and Streptomyces avermitilis reveals that each contains 55 putative eukaryotic-type protein phosphatases (PPs), the largest number ever identified from any single prokaryotic organism. Unlike most other prokaryotic genomes that have only one or two superfamilies of eukaryotic-type PPs, the streptomycete genomes possess the eukaryotic-type PPs that belong to four superfamilies: 2 phosphoprotein phosphatases and 2 low-molecular-mass protein tyrosine phosphatases in each species, 49 Mg 2+ -or Mn 2+ -dependent protein phosphatases (PPMs) and 2 conventional protein tyrosine phosphatases (CPTPs) in S. coelicolor A3(2), and 48 PPMs and 3 CPTPs in S. avermitilis. Sixty-four percent of the PPs found in S. coelicolor A3(2) have orthologues in S. avermitilis, indicating that they originated from a common ancestor and might be involved in the regulation of more conserved metabolic activities. The genes of eukaryotic-type PP unique to each surveyed streptomycete genome are mainly located in two arms of the linear chromosomes and their evolution might be involved in gene acquisition or duplication to adapt to the extremely variable soil environments where these organisms live. In addition, 56 % of the PPs from S. coelicolor A3(2) and 65 % of the PPs from S. avermitilis possess at least one additional domain having a putative biological function. These include the domains involved in the detection of redox potential, the binding of cyclic nucleotides, mRNA, DNA and ATP, and the catalysis of phosphorylation reactions. Because they contained multiple functional domains, most of them were assigned functions other than PPs in previous annotations. Although few studies have been conducted on the physiological functions of the PPs in streptomycetes, the existence of large numbers of putative PPs in these two streptomycete genomes strongly suggests that eukaryotic-type PPs play important regulatory roles in primary or secondary metabolic pathways. The identification and analysis of such a large number of putative eukaryotic-type PPs from S. coelicolor A3(2) and S. avermitilis constitute a basis for further exploration of the signal transduction pathways mediated by these phosphatases in industrially important strains of streptomycetes. INTRODUCTIONReversible protein phosphorylation/dephosphorylation is a universal mechanism used to regulate protein function. Three types of regulatory protein phosphorylation mechanisms, O-, N-and acyl phosphorylation, have been defined, based on the amino acid residue undergoing the covalent modification. Protein O-phosphorylation occurs on the hydroxyl amino acids serine, threonine and tyrosine, while N-and acyl phosphorylation occur on the basic amino acid histidine and the acidic amino acid aspartic acid, respectively (Cozzone, 1988). Protein O-phosphorylation was originally discovered in eukaryotes where it serves as the backbone of the eukaryotic signal transduction network. In contrast, protein N-and acyl phosphorylation were identified ...

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A gene cluster involved in aerial mycelium formation in Streptomyces griseus encodes proteins similar to the response regulators of two-component regulatory systems and membrane translocators

Abstract: Mutants of Streptomyces griseus deficient in A-factor production are sporulation negative, since A-factor is an essential hormonal regulator for the induction of morphological and physiological differentiation in this bacterium. A

Cited by 69 publications

References 46 publications

A novel extracytoplasmic phenol oxidase of Streptomyces: its possible involvement in the onset of morphogenesis The DDBJ accession number for the sequence reported in this paper is AB056583.

A novel extracytoplasmic phenol oxidase of Streptomyces: its possible involvement in the onset of morphogenesis The DDBJ accession number for the sequence reported in this paper is AB056583.

A Novel Transglutaminase Substrate fromStreptomyces mobaraensisTriggers Autolysis of Neutral Metalloproteases

Comparative analysis of eukaryotic-type protein phosphatases in two streptomycete genomes

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