Identification of factor C protein fromStreptomyces griseus by microelectrospray mass spectrometry

Szabó, Pál; Kele, Zoltán; Birkó, Zsuzsa; Szeszák, F; Bíró, Sándor; Janáky, Tamás

doi:10.1002/(sici)1096-9888(199912)34:12<1312::aid-jms885>3.0.co;2-9

Cited by 7 publications

(5 citation statements)

References 22 publications

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“…The effect of factor C is detectable at very low concentrations (c. 1 ng mL À1 ) (Szeszak et al, 1990). Biochemical and DNA sequence information indicate that prefactor C has a 38-aa secretory Tat signal sequence (Biró et al, 1980Szabó et al, 1999). It is therefore likely that factor C acquires its tertiary structure in a cytoplasmic context before export via the Tat system.…”

Section: Factor C: An Extracellular 'Signalling' Proteinmentioning

confidence: 99%

The complex extracellular biology ofStreptomyces

et al. 2010

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Streptomycetes, soil-dwelling mycelial bacteria that form sporulating aerial branches, have an exceptionally large number of predicted secreted proteins, including many exported via the twin-arginine transport system. Their use of noncatalytic substrate-binding proteins and hydrolytic enzymes to obtain soluble nutrients from carbohydrates such as chitin and cellulose enables them to interact with other organisms. Some of their numerous secreted proteases participate in developmentally significant extracellular cascades, regulated by inhibitors, which lead to cannibalization of the substrate mycelium biomass to support aerial growth and sporulation. They excrete many secondary metabolites, including important antibiotics. Some of these play roles in interactions with eukaryotes. Surprisingly, some antibiotic biosynthetic enzymes are extracellular. Antibiotic production is often regulated by extracellular signalling molecules, some of which also control morphological differentiation. Amphipathic proteins, assembled with the help of cellulose-like material, are required for both hyphal attachment to surfaces and aerial reproductive growth. Comparative genomic analysis suggests that the acquisition of genes for extracellular processes has played a huge part in speciation. The rare codon TTA, which is present in the key pleiotropic regulatory gene adpA and many pathway-specific regulatory genes for antibiotic production, has a particular influence on extracellular biology.

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Section: Factor C: An Extracellular 'Signalling' Proteinmentioning

confidence: 99%

The complex extracellular biology ofStreptomyces

et al. 2010

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“…The added factor C rapidly disappears from the culture fluid, probably taken up by the cells (Szeszák et al 1991). As was predicted by computer analysis of the gene, we showed by amino acid sequence analysis (Birkó et al 1999;Szabó et al 1999) of the secreted factor C that it has a signal sequence, which is cleaved off during secretion. Analysis of possible transmembrane regions in factor C and their orientation using several programs including Tmpred (Hofmann & Stoffel 1993) and DAS (Cserzo et al 1997) suggested the likely presence of a transmembrane domain in factor C, with its N-terminus positioned inside the cell and its C-terminus facing outward.…”

Section: How Does Factor C Exert Its Function?mentioning

confidence: 59%

“…Factor C was isolated from the culture fluid of S. griseus 45H which readily sporulates in liquid culture (Szabó et al 1962;Biró et al 1980). Our previous results on the effects of the factor C protein have been summarized and the cloning, sequencing and partial analysis of its gene (designated facC) were published recently (Birkó et al 1999;Szabó et al 1999). The present paper provides a transcriptional analysis of the factor C gene as well as further evidence of its role in regulation of sporulation.…”

Section: Introductionmentioning

confidence: 82%

Untitled

Bíró

Birkó

Wezel

2000

Antonie Van Leeuwenhoek

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Factor C is an extracellular signal protein involved in cellular differentiation in Streptomyces griseus. Nuclease S1 mapping experiments revealed that transcription of the gene takes place from a single promoter in a developmental-stage specific manner. The latter was also confirmed by in vivo promoter probing. The sequence of its promoter suggests that the gene is not transcribed by the major sigma factor. The cloned gene expressed from its own promoter in low- and high-copy-number vectors restored normal sporulation to a bald mutant of Streptomyces griseus. Computer analysis of the amino acid sequence revealed the presence of a transmembrane localization segment with the N-terminus positioned inside the cell. These data fit well into our working model that points at an important role for factor C in the morphogenesis of Streptomyces griseus.

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“…Endogenous autoregulator molecules such as the butyrolacton A factor [1] and factor C play an important role in the regulation of the process. Interestingly, factor C is a protein of 31 038 Da [2,3]. S1 mapping experiments showed that the gene was transcribed at the onset of sporulation.…”

Section: Introductionmentioning

confidence: 99%

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni²⁺affinity column chromatography

Birkó

Schauwecker

Pfennig

et al. 2001

FEMS Microbiology Letters

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Factor C is an unusual extracellular protein capable of inducing cytodifferentiation in certain Streptomyces strains. The protein is produced by Streptomyces griseus 45H at such a low amount that the study of its mode of action was hindered by the shortage of purified protein. We report here the expression of C-terminally hexa-His-tagged factor C in Streptomyces lividans and Escherichia coli. Expression in S. lividans is low while in E. coli it is relatively high, yielding about 5--10 mg of biologically fully active protein per liter culture.

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Identification of factor C protein fromStreptomyces griseus by microelectrospray mass spectrometry

Cited by 7 publications

References 22 publications

The complex extracellular biology ofStreptomyces

The complex extracellular biology ofStreptomyces

Untitled

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni²⁺affinity column chromatography

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Identification of factor C protein fromStreptomyces griseus by microelectrospray mass spectrometry

Cited by 7 publications

References 22 publications

The complex extracellular biology ofStreptomyces

The complex extracellular biology ofStreptomyces

Untitled

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni2+affinity column chromatography

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Expression and rapid one-step purification of biologically active His-tagged factor C by Ni²⁺affinity column chromatography