Glucose repression in Streptomyces coelicolor A3(2): a likely regulatory role for glucose kinase

1994 ◽  
Vol 244 (2) ◽  
pp. 135-143 ◽  
Author(s):  
Susan Angell ◽  
Cinzia G. Lewis ◽  
Mark J. Buttner ◽  
Mervyn J. Bibb

2012 ◽  
Vol 58 (10) ◽  
pp. 1195-1201 ◽  
Author(s):  
Angela Forero ◽  
Mauricio Sánchez ◽  
Adán Chávez ◽  
Beatriz Ruiz ◽  
Romina Rodríguez-Sanoja ◽  
...  

Streptomyces coelicolor mutants resistant to 2-deoxyglucose are insensitive to carbon catabolite repression (CCR). Total reversion to CCR sensitivity is observed by mutant complementation with a DNA region harboring both glucose kinase glkA gene and the sco2127 gene. The sco2127 is located upstream of glkA and encodes a putative protein of 20.1 kDa. In S. coelicolor, actinorhodin production is subject to glucose repression. To explore the possible involvement of both SCO2127 and glucose kinase (Glk) in the glucose sensitivity of actinorhodin production, this effect was evaluated in a wild-type S. coelicolor A3(2) M145 strain and a sco2127 null mutant (Δsco2127) derived from this wild-type strain. In comparison with strain M145, actinorhodin production by the mutant was insensitive to glucose repression. Under repressive conditions, only minor differences were observed in glucose utilization and Glk production between these strains. SCO2127 was detected mainly during the first 36 h of fermentation, just before the onset of antibiotic production, and its synthesis was not related to a particular carbon source. The glucose sensitivity of antibiotic production was restored to wild-type phenotype by transformation with an integrative plasmid containing sco2127. Our results support the hypothesis that SCO2127 is a negative regulator of actinorhodin production and suggest that the effect is independent of Glk.



1998 ◽  
Vol 180 (11) ◽  
pp. 2911-2914 ◽  
Author(s):  
Akihiro Saito ◽  
Takeshi Fujii ◽  
Tadakatsu Yoneyama ◽  
Kiyotaka Miyashita

ABSTRACT Chitinase production in Streptomyces lividans is induced by chitin and repressed in the presence of glucose. A mutant ofS. lividans TK24, strain G015, which was defective in glucose repression of chitinase production, was obtained by screening colonies for zones of clearing on colloidal chitin agar plates containing 1.0% (wt/vol) glucose. The transcriptional analysis ofchiA in G015 with xylE, which encodes catechol 2,3-dioxygenase, as a reporter gene showed that the transcription from the chiA promoter of S. lividans TK24 occurred regardless of the presence of glucose. G015 was resistant to 2-deoxyglucose (2-DOG) and did not utilize glucose as a sole carbon source. When a DNA fragment containing glkA, a gene for glucose kinase, of Streptomyces coelicolor A3(2) was introduced into strain G015 on a low-copy-number plasmid, the sensitivity to 2-DOG, the ability to utilize glucose, and the glucose repression of chitinase production were restored. These results indicate that glkA is involved in glucose repression of chitinase production in S. lividans TK24.





Microbiology ◽  
2010 ◽  
Vol 156 (5) ◽  
pp. 1527-1537 ◽  
Author(s):  
Rosario Pérez-Redondo ◽  
Irene Santamarta ◽  
Roel Bovenberg ◽  
Juan F. Martín ◽  
Paloma Liras

Streptomyces clavuligerus ATCC 27064 is unable to use glucose but has genes for a glucose permease (glcP) and a glucose kinase (glkA). Transformation of S. clavuligerus 27064 with the Streptomyces coelicolor glcP1 gene with its own promoter results in a strain able to grow on glucose. The glcP gene of S. clavuligerus encodes a 475 amino acid glucose permease with 12 transmembrane segments. GlcP is a functional protein when expressed from the S. coelicolor glcP1 promoter and complements two different glucose transport-negative Escherichia coli mutants. Transcription studies indicate that the glcP promoter is very weak and does not allow growth on glucose. These results suggest that S. clavuligerus initially contained a functional glucose permease gene, like most other Streptomyces species, and lost the expression of this gene by adaptation to glucose-poor habitats.



2005 ◽  
Vol 156 (3) ◽  
pp. 361-366 ◽  
Author(s):  
Iveta Imriskova ◽  
Roberto Arreguín-Espinosa ◽  
Silvia Guzmán ◽  
Romina Rodriguez-Sanoja ◽  
Elizabeth Langley ◽  
...  


2001 ◽  
Vol 183 (7) ◽  
pp. 2198-2203 ◽  
Author(s):  
Eung-Soo Kim ◽  
Hee-Jeon Hong ◽  
Cha-Yong Choi ◽  
Stanley N. Cohen

ABSTRACT While the biosynthetic gene cluster encoding the pigmented antibiotic actinorhodin (ACT) is present in the two closely related bacterial species, Streptomyces lividans andStreptomyces coelicolor, it normally is expressed only inS. coelicolor—generating the deep-blue colonies responsible for the S. coelicolor name. However, multiple copies of the two regulatory genes, afsR andafsR2, activate ACT production in S. lividans, indicating that this streptomycete encodes a functional ACT biosynthetic pathway. Here we report that the occurrence of ACT biosynthesis in S. lividans is determined conditionally by the carbon source used for culture. We found that the growth ofS. lividans on solid media containing glucose prevents ACT production in this species by repressing the synthesis ofafsR2 mRNA; a shift to glycerol as the sole carbon source dramatically relieved this repression, leading to extensive ACT synthesis and obliterating this phenotypic distinction between S. lividans and S. coelicolor. Transcription from theafsR2 promoter during growth in glycerol was dependent onafsR gene function and was developmentally regulated, occurring specifically at the time of aerial mycelium formation and coinciding temporally with the onset of ACT production. In liquid media, where morphological differentiation does not occur, ACT production in the absence of glucose increased as S. lividans cells entered stationary phase, but unlike ACT biosynthesis on solid media, occurred by a mechanism that did not require either afsR or afsR2. Our results identify parallel medium-dependent pathways that regulate ACT biosynthesis in S. lividans and further demonstrate that the production of this antibiotic in S. lividans grown on agar can be modulated by carbon source through the regulation ofafsR2 mRNA synthesis.



2003 ◽  
Vol 185 (3) ◽  
pp. 929-937 ◽  
Author(s):  
Harald Nothaft ◽  
Stephan Parche ◽  
Annette Kamionka ◽  
Fritz Titgemeyer

ABSTRACT HPr, the histidine-containing phosphocarrier protein of the bacterial phosphotransferase system (PTS), serves multiple functions in carbohydrate uptake and carbon source regulation in low-G+C-content gram-positive bacteria and in gram-negative bacteria. To assess the role of HPr in the high-G+C-content gram-positive organism Streptomyces coelicolor, the encoding gene, ptsH, was deleted. The ptsH mutant BAP1 was impaired in fructose utilization, while growth on other carbon sources was not affected. Uptake assays revealed that BAP1 could not transport appreciable amounts of fructose, while the wild type showed inducible high-affinity fructose transport with an apparent Km of 2 μM. Complementation and reconstitution experiments demonstrated that HPr is indispensable for a fructose-specific PTS activity. Investigation of the putative fruKA gene locus led to identification of the fructose-specific enzyme II permease encoded by the fruA gene. Synthesis of HPr was not specifically enhanced in fructose-grown cells and occurred also in the presence of non-PTS carbon sources. Transcriptional analysis of ptsH revealed two promoters that are carbon source regulated. In contrast to what happens in other bacteria, glucose repression of glycerol kinase was still operative in a ptsH background, which suggests that HPr is not involved in general carbon regulation. However, fructose repression of glycerol kinase was lost in BAP1, indicating that the fructose-PTS is required for transduction of the signal. This study provides the first molecular genetic evidence of a physiological role of the PTS in S. coelicolor.



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