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Forkhead-associated proteins genetically linked to the serine/threonine kinase PknB regulate carbon flux towards antibiotic biosynthesis in Streptomyces coelicolor.

Jones G, Del Sol R, Dudley E, Dyson P - Microb Biotechnol (2010)

Bottom Line: Here we report functional analysis of pknB and two linked genes, fhaAB, encoding forkhead-associated (FHA) domain proteins that are part of a highly conserved gene locus in actinobacteria.FhaAB are candidate interacting partners of PknB and loss of their function resulted in deregulation of central carbon metabolism, with carbon flux diverted to synthesis of the antibiotic actinorhodin.The results indicate that inactivation of FHA 'brake' proteins can potentially amplify the function of STPKs and, in this case, provide a means to overproduce antibiotics.

View Article: PubMed Central - PubMed

Affiliation: Institute of Life Science, Swansea University, Singleton Park, Swansea SA28PP, UK.

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Increased actinorhodin production by pknB and fhaAB mutants. The yields of actinorhodin and γ‐actinorhodin at indicated time points relative to cell density (OD450) were plotted for cultures grown in liquid R5 with or without addition of 250 mM NaCl. The values are averages of three independent experiments and standard deviations were <5% of the plotted values. (/□) M145/ + NaCl; (▴/▵) pknB/ + NaCl; (●/○) fhaAB/ + NaCl.
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f2: Increased actinorhodin production by pknB and fhaAB mutants. The yields of actinorhodin and γ‐actinorhodin at indicated time points relative to cell density (OD450) were plotted for cultures grown in liquid R5 with or without addition of 250 mM NaCl. The values are averages of three independent experiments and standard deviations were <5% of the plotted values. (/□) M145/ + NaCl; (▴/▵) pknB/ + NaCl; (●/○) fhaAB/ + NaCl.

Mentions: Increased production of actinorhodin by the pknB mutant was quantified during growth in submerged culture. The mutant produced approximately four times the yield of the parental strain (Fig. 2), but the overall growth rate was unaffected. We have previously observed that addition of osmolyte stimulates production of actinorhodin by the parental strain M145 (Bishop et al., 2004). However, in contrast, actinorhodin production by the pknB mutant was partly suppressed by addition of osmolyte (Fig. 2).


Forkhead-associated proteins genetically linked to the serine/threonine kinase PknB regulate carbon flux towards antibiotic biosynthesis in Streptomyces coelicolor.

Jones G, Del Sol R, Dudley E, Dyson P - Microb Biotechnol (2010)

Increased actinorhodin production by pknB and fhaAB mutants. The yields of actinorhodin and γ‐actinorhodin at indicated time points relative to cell density (OD450) were plotted for cultures grown in liquid R5 with or without addition of 250 mM NaCl. The values are averages of three independent experiments and standard deviations were <5% of the plotted values. (/□) M145/ + NaCl; (▴/▵) pknB/ + NaCl; (●/○) fhaAB/ + NaCl.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3818866&req=5

f2: Increased actinorhodin production by pknB and fhaAB mutants. The yields of actinorhodin and γ‐actinorhodin at indicated time points relative to cell density (OD450) were plotted for cultures grown in liquid R5 with or without addition of 250 mM NaCl. The values are averages of three independent experiments and standard deviations were <5% of the plotted values. (/□) M145/ + NaCl; (▴/▵) pknB/ + NaCl; (●/○) fhaAB/ + NaCl.
Mentions: Increased production of actinorhodin by the pknB mutant was quantified during growth in submerged culture. The mutant produced approximately four times the yield of the parental strain (Fig. 2), but the overall growth rate was unaffected. We have previously observed that addition of osmolyte stimulates production of actinorhodin by the parental strain M145 (Bishop et al., 2004). However, in contrast, actinorhodin production by the pknB mutant was partly suppressed by addition of osmolyte (Fig. 2).

Bottom Line: Here we report functional analysis of pknB and two linked genes, fhaAB, encoding forkhead-associated (FHA) domain proteins that are part of a highly conserved gene locus in actinobacteria.FhaAB are candidate interacting partners of PknB and loss of their function resulted in deregulation of central carbon metabolism, with carbon flux diverted to synthesis of the antibiotic actinorhodin.The results indicate that inactivation of FHA 'brake' proteins can potentially amplify the function of STPKs and, in this case, provide a means to overproduce antibiotics.

View Article: PubMed Central - PubMed

Affiliation: Institute of Life Science, Swansea University, Singleton Park, Swansea SA28PP, UK.

Show MeSH
Related in: MedlinePlus