Archives of Microbiology

, Volume 182, Issue 2–3, pp 165–174 | Cite as

The role of the sulfur globule proteins of Allochromatium vinosum: mutagenesis of the sulfur globule protein genes and expression studies by real-time RT-PCR

  • Alexander Prange
  • Harald Engelhardt
  • Hans G. Trüper
  • Christiane DahlEmail author
Original Paper


During oxidation of reduced sulfur compounds, the purple sulfur bacterium Allochromatium vinosum stores sulfur in the periplasm in the form of intracellular sulfur globules. The sulfur in the globules is enclosed by a protein envelope that consists of the homologous 10.5-kDa proteins SgpA and SgpB and the smaller 8.5-kDa SgpC. Reporter gene fusions of sgpA and alkaline phosphatase showed the constitutive expression of sgpA in A. vinosum and yielded additional evidence for the periplasmic localization of the sulfur globules. Expression analysis of the wild-type sgp genes by quantitative RT-PCR using the LightCycler system showed the constitutive expression of all three sgp genes. The expression of sgpB and sgpC is significantly enhanced under photolithotrophic conditions. Interestingly, sgpB is expressed ten times less than sgpA and sgpC implying that SgpA and SgpC are the “main proteins” of the sulfur globule envelope. Mutants with inactivated sgpA or sgpB did not show any differences in comparison with the wild-type, i.e., the encoded proteins can replace each other, whereas inactivation of sgpC leads to the formation of considerably smaller sulfur globules. This indicates a role of SgpC for globule expansion. A sgpBC double mutant was unable to grow on sulfide and could not form sulfur globules, showing that the protein envelope is indispensible for the formation and deposition of intracellular sulfur.


Allochromatium vinosum Sulfur globule proteins Sulfide oxidation Sulfur globules Phototrophic sulfur bacteria 



Sulfur globule protein


Sulfur globule protein gene



We thank Daniel C Brune (Arizona State University, Tempe, USA) for useful hints concerning HPLC analysis of the sulfur globule proteins, Brigitte Kühlmorgen for skilfull technical assistance with electron microscopy, and Kobchai Pattaragulwanit (Chulalongkorn University, Bangkok, Thailand) for helpful discussions. AP thanks the GEN-IAL GmbH (Troisdorf) for the possibility to perform the LightCycler experiments in their laboratory and the Stiftung der Deutschen Wirtschaft (Studienförderwerk Klaus Murmann) for a doctoral scholarship. This work was supported by the Deutsche Forschungsgemeinschaft (DFG grant Tr 133/26-1,2,3) and the Fonds der Chemischen Industrie (HGT).


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Copyright information

© Springer-Verlag 2004

Authors and Affiliations

  • Alexander Prange
    • 1
    • 2
    • 3
  • Harald Engelhardt
    • 4
  • Hans G. Trüper
    • 1
  • Christiane Dahl
    • 1
    Email author
  1. 1.Institut für Mikrobiologie & BiotechnologieRheinische Friedrich-Wilhelms-Universität BonnBonnGermany
  2. 2.Institut für Pflanzenkrankheiten, Abteilung Landwirtschaftliche und Lebensmittel-MikrobiologieRheinische Friedrich-Wilhelms-Universität BonnBonnGermany
  3. 3.IBELIN GbRBrilonGermany
  4. 4.Max-Planck-Institut für BiochemieMartinsriedGermany

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