Streptococcus mutans GlnK protein: an unusual PII family member
Streptococcus mutans is a Gram-positive bacterium present in the oral cavity, and is considered to be one of the leading causes of dental caries. S. mutans has a glnK gene, which codes for a PII-like protein that is possibly involved in the integration of carbon, nitrogen and energy metabolism in se...
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| Published in: | Brazilian journal of medical and biological research Vol. 44; no. 5; pp. 394 - 401 |
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| Abstract | Streptococcus mutans is a Gram-positive bacterium present in the oral cavity, and is considered to be one of the leading causes of dental caries. S. mutans has a glnK gene, which codes for a PII-like protein that is possibly involved in the integration of carbon, nitrogen and energy metabolism in several organisms. To characterize the GlnK protein of S. mutans, the glnK gene was amplified by PCR, and cloned into the expression vectors pET29a(+) and pET28b(+). The native GlnK-Sm was purified by anion exchange (Q-Sepharose) and affinity (Hi-Trap Heparin) chromatography. The GlnK-His-Sm protein was purified using a Hi-Trap Chelating-Ni2+ column. The molecular mass of the GlnK-His-Sm proteins was 85 kDa as determined by gel filtration, indicating that this protein is a hexamer in solution. The GlnK-His-Sm protein is not uridylylated by the Escherichia coli GlnD protein. The activities of the GlnK-Sm and GlnK-His-Sm proteins were assayed in E. coli constitutively expressing the Klebsiella pneumoniae nifLA operon. In K. pneumoniae, NifL inhibits NifA activity in the presence of high ammonium levels and the GlnK protein is required to reduce the inhibition of NifL in the presence of low ammonium levels. The GlnK-Sm protein was unable to reduce NifL inhibition of NifA protein. Surprisingly, the GlnK-His-Sm protein was able to partially reduce NifL inhibition of the NifA protein under nitrogen-limiting conditions, in a manner similar to the GlnK protein of E. coli. These results suggested that S. mutans GlnK is functionally different from E. coli PII proteins. |
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| AbstractList | Streptococcus mutans is a Gram-positive bacterium present in the oral cavity, and is considered to be one of the leading causes of dental caries. S. mutans has a glnK gene, which codes for a PII-like protein that is possibly involved in the integration of carbon, nitrogen and energy metabolism in several organisms. To characterize the GlnK protein of S. mutans, the glnK gene was amplified by PCR, and cloned into the expression vectors pET29a(+) and pET28b(+). The native GlnK-Sm was purified by anion exchange (Q-Sepharose) and affinity (Hi-Trap Heparin) chromatography. The GlnK-His-Sm protein was purified using a Hi-Trap Chelating-Ni2+ column. The molecular mass of the GlnK-His-Sm proteins was 85 kDa as determined by gel filtration, indicating that this protein is a hexamer in solution. The GlnK-His-Sm protein is not uridylylated by the Escherichia coli GlnD protein. The activities of the GlnK-Sm and GlnK-His-Sm proteins were assayed in E. coli constitutively expressing the Klebsiella pneumoniae nifLA operon. In K. pneumoniae, NifL inhibits NifA activity in the presence of high ammonium levels and the GlnK protein is required to reduce the inhibition of NifL in the presence of low ammonium levels. The GlnK-Sm protein was unable to reduce NifL inhibition of NifA protein. Surprisingly, the GlnK-His-Sm protein was able to partially reduce NifL inhibition of the NifA protein under nitrogen-limiting conditions, in a manner similar to the GlnK protein of E. coli. These results suggested that S. mutans GlnK is functionally different from E. coli PII proteins. Streptococcus mutans is a Gram-positive bacterium present in the oral cavity, and is considered to be one of the leading causes of dental caries. S. mutans has a glnK gene, which codes for a PII-like protein that is possibly involved in the integration of carbon, nitrogen and energy metabolism in several organisms. To characterize the GlnK protein of S. mutans, the glnK gene was amplified by PCR, and cloned into the expression vectors pET29a(+) and pET28b(+). The native GlnK-Sm was purified by anion exchange (Q-Sepharose) and affinity (Hi-Trap Heparin) chromatography. The GlnK-His-Sm protein was purified using a Hi-Trap Chelating-Ni super(2+) column. The molecular mass of the GlnK-His-Sm proteins was 85 kDa as determined by gel filtration, indicating that this protein is a hexamer in solution. The GlnK-His-Sm protein is not uridylylated by the Escherichia coli GlnD protein. The activities of the GlnK-Sm and GlnK-His-Sm proteins were assayed in E. coli constitutively expressing the Klebsiella pneumoniae nifLA operon. In K. pneumoniae, NifL inhibits NifA activity in the presence of high ammonium levels and the GlnK protein is required to reduce the inhibition of NifL in the presence of low ammonium levels. The GlnK-Sm protein was unable to reduce NifL inhibition of NifA protein. Surprisingly, the GlnK-His-Sm protein was able to partially reduce NifL inhibition of the NifA protein under nitrogen-limiting conditions, in a manner similar to the GlnK protein of E. coli. These results suggested that S. mutans GlnK is functionally different from E. coli PII proteins. |
| Author | Portugal, M.E.G. Benelli, E.M. Souza, E.M. Pedrosa, F.O. |
| AuthorAffiliation | Universidade Federal do Paraná |
| AuthorAffiliation_xml | – name: Universidade Federal do Paraná |
| Author_xml | – sequence: 1 givenname: M.E.G. surname: Portugal fullname: Portugal, M.E.G. organization: Universidade Federal do Paraná, Brasil – sequence: 2 givenname: E.M. surname: Souza fullname: Souza, E.M. organization: Universidade Federal do Paraná, Brasil – sequence: 3 givenname: F.O. surname: Pedrosa fullname: Pedrosa, F.O. organization: Universidade Federal do Paraná, Brasil – sequence: 4 givenname: E.M. surname: Benelli fullname: Benelli, E.M. organization: Universidade Federal do Paraná, Brasil |
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| CitedBy_id | crossref_primary_10_1111_j_1574_6976_2012_00351_x crossref_primary_10_1590_S0100_879X2011007500138 |
| Cites_doi | 10.1046/j.1365-2958.2001.02243.x 10.1016/S0021-9258(18)46926-8 10.1038/nrmicro1772 10.1016/S0076-6879(85)13032-6 10.1093/protein/1.1.67 10.1007/978-1-4419-1528-3_5 10.1002/prot.1168 10.1128/jb.179.23.7446-7455.1997 10.1074/jbc.M312399200 10.1111/j.1365-2958.2005.04511.x 10.1016/j.resmic.2005.01.015 10.1016/S0378-1097(99)00497-8 10.1093/emboj/16.18.5562 10.1038/nrmicro954 10.1016/S0968-0004(00)89080-5 10.1073/pnas.172501299 10.1002/elps.1150080203 10.1046/j.1365-2958.1998.00932.x 10.1128/jb.184.4.1028-1040.2002 10.1046/j.1365-2958.2002.03149.x 10.1128/JB.180.24.6661-6667.1998 10.1128/MMBR.59.4.604-622.1995 10.1046/j.1365-2958.1996.6281349.x 10.1021/bi901158h 10.1128/jb.175.21.6737-6744.1993 10.1046/j.1365-2958.2002.03150.x 10.1016/0003-2697(76)90527-3 10.1128/jb.176.1.84-91.1994 10.1021/bi9011594 10.1128/JB.150.1.214-220.1982 10.1073/pnas.0602278103 10.1128/jb.173.24.7741-7749.1991 10.1016/S0168-9525(99)01887-9 10.1111/j.1365-2958.1993.tb01706.x 10.1093/bioinformatics/btm404 10.1128/jb.179.14.4623-4626.1997 |
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| Keywords | GlnK Nitrogen metabolism Streptococcus mutans |
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| Title | Streptococcus mutans GlnK protein: an unusual PII family member |
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