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J Bacteriol, June 1998, p. 2911-2914, Vol. 180, No. 11
National Institute of Agro-Environmental
Sciences,
Received 30 December 1997/Accepted 3 April 1998
Chitinase production in Streptomyces lividans is
induced by chitin and repressed in the presence of glucose. A mutant of
S. 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 of
chiA 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.
Streptomyces species are
saprophytic soil bacteria and are well known as decomposers of chitin,
which is hydrolyzed by chitinase (EC 3.2.1.14). Many chitinase genes of
Streptomyces have been cloned and sequenced (3, 7,
18-20, 23-25, 29). Their expression is induced by chitin and
repressed by glucose (7, 19, 25). A pair of 12-bp direct
repeats present in the promoter regions of all the known chitinase
genes from Streptomyces (20) are implicated in
the regulation of chitinase gene expression (5, 22). This
suggests that there exists a common regulatory mechanism for induction
and repression of chitinase genes in Streptomyces. Recently,
reg1, a regulatory gene for amylase production in
Streptomyces lividans, has been reported to be involved in
the regulation of chitinase production as well (21).
However, the mechanism of glucose repression of chitinase gene
expression in Streptomyces is still not understood.
Mutants of Streptomyces coelicolor A3(2) that are resistant
to 2-deoxyglucose (2-DOG) (8) are defective in glucose
kinase activity (27) and relieved of glucose repression of
several catabolite pathways, including sugar utilization
(8), glycerol utilization (27), agarase
production (10), and amylase production (31).
These data indicate that glucose kinase plays a central role in glucose
repression in S. coelicolor A3(2). The glkA gene of S. coelicolor A3(2), encoding glucose kinase
(2), restores 2-DOG sensitivity and glucose repression of
dagAp4 transcription (2) in
2-DOG-resistant mutants. However, Ingram and Westpheling (13) reported that glkA is not required for
glucose repression of the chi63 promoter of
Streptomyces plicatus (25) in a
ccrA1-glkA double mutant of S. coelicolor A3(2).
We isolated mutants of S. lividans TK24 defective in glucose
repression of chitinase production by using colloidal chitin agar
plates containing glucose. The mutants made clear zones around their
colonies, while their parental strain, TK24, did not. G015, one of the
mutants defective in glucose repression of chitinase production, was
resistant to 2-DOG and did not utilize glucose as a sole carbon source,
suggesting that it contained the mutation in glkA. After
studying this mutant, we report here that glkA is involved
in glucose repression of chitinase production in S. lividans.
Bacterial strains and plasmids.
Bacterial strains and
plasmids used in this study are shown in Table
1. Plasmid pEMX151, a derivative of the
low-copy-number plasmid pXE4 (11), was used for
transcriptional analysis of the chiA promoter from S. lividans. The BamHI-HindIII fragment of
pXE4 located upstream of the xylE reporter gene was replaced with a fragment of about 1 kb containing the DNA sequence extending from ca. 500 bp upstream to ca. 500 bp downstream of the transcription initiation site of chiA (17). pXE4 was used to
construct pGA01 and pGA02. A 1.2-kb fragment including the coding
region and one of the two promoters of glkA of S. coelicolor A3(2) was generated by digesting pIJ2423 (2)
with BglII, ligated to the BamHI site of pXE4,
and introduced into Escherichia coli XL1-Blue by
transformation. The orientations of glkA were determined
from the digestion patterns with HindIII. The
glkA gene was inserted in the same orientation as the
xylE reporter gene in pGA01 and in the opposite orientation in pGA02. pGAH01 was constructed by ligating the 1.2-kb
BglII fragment containing glkA into the
BamHI site of the high-copy-number vector pIJ486 and
introduced into S. lividans TK24 by transformation.
Manipulation of DNA.
Protoplast preparation and
transformation of S. lividans was performed according to the
method of Hopwood et al. (9). Plasmids were prepared by the
alkaline lysis method (9, 26). All procedures involving
recombinant DNA were carried out as described by Sambrook et al.
(26).
Isolation of S. lividans mutants.
Spores of
S. lividans TK24 were irradiated with UV light (wavelength,
302 nm) to 0.4% survival and spread in the dark (9) on ISCG
agar medium [0.15% (wt/vol) colloidal chitin, 5 mM MgSO4, 15 mM (NH4)2SO4, 25 mM
N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid (TES;
pH 7.2), 0.5 mM NaH2PO4, 0.5 mM
K2HPO4, 0.1% (vol/vol) trace element solution
(0.1 g each of ZnSO4-7H2O,
FeSO4-7H2O, MnCl2-4H2O,
and NaCl per liter), 1.0% (wt/vol) glucose, and 1.5% (wt/vol) agar].
Colloidal chitin was prepared by the method of Lingappa and Lockwood
(16). After 4 weeks of incubation at 30°C in the dark,
colonies with clear zones around them were picked up and streaked on
SFM agar medium (30).
2-DOG sensitivity and glucose utilization.
To test
resistance to 2-DOG, spores formed on SFM agar medium were spotted on
NMMB agar medium (8) containing 10 mM arabinose with or
without 100 mM 2-DOG. For G015 containing derivatives of pXE4, the agar
media were supplemented with 50 µg of thiostrepton/ml. After
incubation for 5 days at 30°C, resistance to 2-DOG was judged from
the sizes of the colonies. The ability to utilize glucose was
determined from growth on NMMB agar medium containing 1.0% (wt/vol)
glucose or in SMM liquid medium without polyethylene glycol 1000 and
casamino acids (28) but containing 1.0% (wt/vol) glucose as
a sole carbon source. On the agar plates, the sizes of colonies of G015
and its derivatives were compared with those of TK24 and its
derivatives, respectively. Agar medium supplemented with 50 µg of
thiostrepton/ml was used for G015 containing derivatives of pXE4.
Germinated spores (9) were inoculated and grown at 30°C
with shaking at 200 rpm. One-milliliter portions of the culture fluid
were sampled periodically, and the mycelia were harvested by
centrifugation. Growth was monitored by the protein content of the
mycelia, measured as follows. The pellet was washed with distilled
water (MiliQ), resuspended in MiliQ, and sonicated on ice. One-half
volume of 3 N NaOH was added to the sonicated lysate, and after
incubation for 30 min at 100°C, the lysate was centrifuged at 10,000 rpm (M150; SAKUMA) (ca. 7,000 × g) for 10 min at room temperature. The protein concentration of the supernatant was measured
by the method of Bradford (4) with bovine plasma gamma globulin as the protein standard, and the amount of protein per milliliter of culture was calculated.
Chitinase assay.
Twenty milliliters of Luria-Bertani (LB)
liquid medium (26) was inoculated with germinated spores and
incubated at 30°C for 48 h with shaking at 150 rpm. For strains
containing pXE4 derivatives or pIJ486 derivatives, the medium was
supplemented with 2 or 5 µg of thiostrepton/ml, respectively. The
culture was divided into three aliquots. Mycelia in each aliquot were
harvested by centrifugation and washed with 10 ml of YE medium (0.7 g
of K2HSO4, 0.3 g of
KH2SO4, 0.5 g of MgSO4,
0.01 g of FeSO4, 0.3 g of
NH4NO3, and 1.0 g of yeast extract per
liter). The mycelia were resuspended in an equal volume of YE medium,
YE medium with 0.05% (wt/vol) colloidal chitin, or YE medium with
0.05% (wt/vol) colloidal chitin and 1.0% (wt/vol) glucose. The
protein content of 1 ml of culture was measured as described above, and
the inocula were adjusted to about 100 µg of protein per ml. The
cultures were grown at 30°C with shaking. A 0.5-ml portion of the
culture fluid was sampled periodically and stored at Catechol dioxygenase assay.
The transformants TK24(pEMX151)
and G015(pEMX151) were cultured as described in "Chitinase
assay" above with the exception that G015(pEMX151) was
precultured in LB medium containing 2 µg of thiostrepton/ml for
72 h. The longer preculture period of G015(pEMX151) was due to
the slower growth rate of G015(pEMX151) compared to that of
TK24(pEMX151). The cell extracts were prepared, and catechol 2,3-dioxygenase activity was measured spectrophotometrically as described previously (12, 32). Catechol 2,3-dioxygenase
activity was expressed as the rate of increase in optical density at
375 nm per minute per milligram of protein.
Glucose kinase assay.
Glucose kinase activity measurements
were done as described by Angell et al. (2).
Southern hybridization.
Total DNA was prepared as described
by Hopwood et al. (9). Two micrograms of the DNA was
digested with BclI, electrophoresed in 0.8% (wt/vol)
agarose gel, and transferred to a Hybond N+ membrane (Amersham). The
1.2-kb BglII fragment containing glkA from
S. coelicolor A3(2), which was prepared from pIJ2423, was
used as a probe. Hybridization was performed with digoxigenin
(Boehringer Mannheim) by following the manufacturer's instructions.
G015 is defective in glucose repression of chitinase
production.
To isolate mutants of S. lividans TK24
defective in glucose repression of chitinase production, UV-irradiated
spores were spread on ISCG agar medium. After 3 weeks of incubation at
30°C, several colonies among approximately 5,000 had clear zones
around them and one, G015, was resistant to 2-DOG (see below). The
phenotype of G015 on ISCG medium was confirmed after single-colony
purification. Chitinase production by G015 was then compared with that
of TK24 in liquid medium. Chitinase production by G015 was induced by the addition of 0.05% (wt/vol) colloidal chitin regardless of the
presence of glucose, whereas TK24 did not produce chitinase in the
presence of glucose (Fig. 1A). These
results indicated that G015 was defective in glucose repression of
chitinase production.
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
glkA Is Involved in Glucose Repression
of Chitinase Production in Streptomyces lividans
ABSTRACT
Top
Abstract
Introduction
Materials & Methods
Results
Discussion
References
INTRODUCTION
Top
Abstract
Introduction
Materials & Methods
Results
Discussion
References
MATERIALS AND METHODS
Top
Abstract
Introduction
Materials & Methods
Results
Discussion
References
TABLE 1.
Bacterial strains and plasmids used in this study
80°C. The
samples were thawed and centrifuged, and chitinase activity was
measured in the culture supernatant as described previously
(19), using the fluorogenic substrate
4-methylumbelliferyl-N,N',-diacetyl chitobioside
[4MU-(GlcNAc)2] or
4-methylumbelliferyl-N,N',N"-triacetyl chitotrioside [4MU-(GlcNAc)3] (Sigma). One unit of
chitinase activity was defined as described by Miyashita et al.
(19). Chitinase activity was expressed in units per
microgram of mycelial protein.
RESULTS
Top
Abstract
Introduction
Materials & Methods
Results
Discussion
References
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FIG. 1.
Chitinase activity induced by colloidal chitin in the
presence or absence of glucose in S. lividans TK24 and G015
(A); in TK24(pXE4), G015(pXE4), and G015(pGA01) (B); and in
TK24(pGAH01) (C). Chitinase activity was measured with
4MU-(GlcNAc)2 for panel A and 4MU-(GlcNAc)3 for
panels B and C. At time zero, cultures grown in LB medium at 30°C for
48 h were divided into three aliquots, and the mycelia in each
aliquot were suspended in YE medium (open triangles), YE medium plus
0.05% (wt/vol) colloidal chitin (open circles), or YE medium plus
0.05% (wt/vol) colloidal chitin plus 1.0% (wt/vol) glucose (solid
circles).
Glucose repression of chiA transcription is not observed in G015. To investigate the regulation of chitinase gene expression in G015, the levels of transcription from the chiA promoter in TK24 and G015 were compared by using xylE, which encodes catechol 2,3-dioxygenase, as a reporter gene. As shown in Fig. 2, in G015(pEMX151) transcription from the chiA promoter occurred in the presence of colloidal chitin regardless of the presence of glucose, whereas glucose strongly repressed the transcription of chiA in TK24(pEMX151). The level of expression of the chiA promoter in G015(pEMX151) in the presence of colloidal chitin and glucose was 2 to 3 times greater than that observed in the presence of colloidal chitin alone.
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A375 indicates the increase in
optical density per minute at 375 nm. N, YE medium; C, YE medium plus
0.05% (wt/vol) colloidal chitin; CG, YE medium plus 0.05% (wt/vol)
colloidal chitin plus 1.0% (wt/vol) glucose.
G015 was resistant to 2-DOG and did not utilize glucose. G015 grew on NMMB agar medium containing 10 mM arabinose regardless of the presence of 100 mM 2-DOG, whereas TK24 did not grow in the presence of 2-DOG. On NMMB agar medium containing 1.0% (wt/vol) glucose as a sole carbon source, G015 grew poorly compared to TK24. In SMM liquid medium containing 1.0% (wt/vol) glucose as a sole carbon source, G015 did not grow at all. The resistance to 2-DOG and the defect in glucose utilization suggested that the glkA gene was defective in G015 as shown in S. coelicolor A3(2) (2).
glkA restored 2-DOG sensitivity, glucose utilization, and glucose repression in G015. Angell et al. (2) showed that integration of a wild-type glkA gene into the chromosome of a 2-DOG-resistant mutant of S. coelicolor A3(2) restored 2-DOG sensitivity, glucose utilization, and glucose repression of dagAp4. To examine whether the glkA gene restored these three phenotypes in G015, the glkA gene of S. coelicolor A3(2) was introduced into G015. A low-copy-number plasmid, pGA01 (a derivative of pXE4), that contained glkA was constructed. G015 and TK24 were transformed with pGA01 or pXE4, and G015(pXE4), G015(pGA01), and TK24(pXE4) were obtained. The glucose kinase activity of G015(pXE4) was 1/10 that of TK24(pXE4), while G015(pGA01) had approximately the same level as TK24(pXE4) (Table 2). In contrast to G015(pXE4), G015(pGA01) grew well on NMMB agar medium containing 1.0% (wt/vol) glucose and showed no growth in the presence of 100 mM 2-DOG, like TK24(pXE4) (Table 2). These data indicate that G015 is a glucose kinase mutant of S. lividans. Moreover, G015(pGA01) did not produce chitinase when glucose was supplied together with colloidal chitin (Fig. 1B). When pGA02, with glkA in the opposite orientation, was introduced into G015, the same results were obtained (data not shown). Thus, glkA restores glucose repression of chitinase production in G015, and it appears that glkA is involved in glucose repression of chitinase production in S. lividans TK24.
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Introduction of glkA on a high-copy-number plasmid relieves glucose repression of chitinase production in S. lividans. Introduction of glkA on a high-copy-number plasmid relieves glucose repression in S. coelicolor A3(2) (1, 14). The same phenomenon might be expected in S. lividans if glkA is involved in glucose repression of chitinase production in that species. To assess this, the high-copy-number plasmid pGAH01, a derivative of pIJ486 with a 1.2-kb BglII fragment containing glkA of S. coelicolor A3(2), was constructed and introduced into S. lividans TK24 by protoplast transformation. Chitinase production in the presence of glucose was measured in liquid culture. Chitinase production in TK24(pGAH01) was relieved of glucose repression (Fig. 1C). This result strongly supports the involvement of glkA in glucose repression of chitinase production.
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DISCUSSION |
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Top
Abstract
Introduction
Materials & Methods
Results
Discussion
References
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G015, a mutant of S. lividans TK24 that was defective in glucose repression of chitinase production was isolated. G015 showed 2-DOG resistance, no growth in medium that contained glucose as a sole carbon source, and low glucose kinase activity. The glkA gene of S. coelicolor A3(2) restored 2-DOG sensitivity, glucose utilization, and glucose kinase activity to approximately wild-type levels in G015 (Table 2). These data indicate that G015 possesses a mutated glucose kinase gene. The glk locus of S. coelicolor A3(2) is relatively unstable, with a high spontaneous mutation frequency. Spontaneous 2-DOG-resistant mutants show deletion in the glk locus (6). However, Southern analysis revealed that glkA was not deleted in G015, and the signal obtained with G015 was the same as those in S. lividans TK24 and S. coelicolor A3(2) (data not shown). Thus, the mutation of glkA in G015 is likely to be a UV-induced point mutation.
The fact that a glk mutant of S. lividans is relieved of glucose repression of chitinase production suggests the involvement of glkA in glucose repression in S. lividans. Consistent with this, the glkA gene of S. coelicolor A3(2) restored glucose repression of chitinase production in G015 when cloned on a low-copy-number plasmid (Fig. 1B). Moreover, introduction of glkA on a high-copy-number plasmid resulted in the relief of glucose repression of chitinase production in S. lividans TK24 (Fig. 1C). This is also consistent with the relief of glucose repression of dagAp4 transcription when glkA is overexpressed in S. coelicolor A3(2) M145 (1).
The expression level of the chiA promoter in G015 (pEMX151) in the presence of colloidal chitin and glucose was about twice that observed on colloidal chitin alone (Fig. 2B). A similar stimulatory effect from loss of glkA was observed for dagAp4 transcription in S. coelicolor (1). Hodgson (8) showed that most of the glk mutants of S. coelicolor A3(2) which do not utilize glucose as a sole carbon source can transport glucose. Considering that G015 is a glk mutant which cannot utilize glucose, although it is a derivative of S. lividans TK24, it is conceivable that the process of glucose transport or glucose itself stimulates the expression of chiA in G015.
Ingram and Westpheling (13) reported that glkA of S. coelicolor A3(2) is not required for glucose repression of the chi63 promoter of S. plicatus (25), based on a ccrA1-glkA double mutant of S. coelicolor A3(2). This is in contrast to the conclusion obtained in this study of S. lividans. To confirm the involvement of the glkA gene in glucose repression of chitinase production in S. coelicolor, we examined the native chitinase production of a glk mutant of S. coelicolor A3(2) in liquid medium that contained colloidal chitin with or without glucose. Chitinase production in J1668, a glkA deletion mutant of J1508 (10), was repressed in the presence of glucose in liquid media (data not shown), consistent with the finding of Ingram and Westpheling (13). Thus, it seems that the mechanism of glucose repression of chitinase production in S. coelicolor A3(2) is different from that in S. lividans, which is surprising given that they are very closely related species (15) and possess nearly identical chitinase genes (unpublished data).
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ACKNOWLEDGMENTS |
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We are grateful to M. J. Bibb (John Innes Centre, Norwich, United Kingdom) for valuable discussions and for providing J1668 and pIJ2423.
This work was supported in part by a Grant-in-Aid (Bio Design Program 6201) from the Ministry of Agriculture, Forestry, and Fisheries of Japan.
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FOOTNOTES |
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* Corresponding author. Mailing address: National Institute of Agro-Environmental Sciences, 3-1-1 Kan-nondai, Tsukuba, Ibaraki 305-8604, Japan. Phone and fax: (81) 298388256. E-mail: kmiyas{at}ss.niaes.affrc.go.jp.
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REFERENCES |
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Top
Abstract
Introduction
Materials & Methods
Results
Discussion
References
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