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J. Biol. Chem., Vol. 276, Issue 24, 21053-21061, June 15, 2001
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From the Centro de Investigaciones Biológicas, CSIC,
Velázquez 144, 28006 Madrid, Spain
The type 37 capsule of Streptococcus
pneumoniae is a homopolysaccharide built up from repeating units
of
[
Tts, a Processive
-Glucosyltransferase of Streptococcus
pneumoniae, Directs the Synthesis of the Branched Type 37 Capsular Polysaccharide in Pneumococcus and Other Gram-positive
Species*
,
-D-Glcp-(1
2)]--D-Glcp-(13). The elements governing the expression of the tts gene,
coding for the glucosyltransferase involved in the synthesis of the
type 37 pneumococcal capsular polysaccharide, have been studied. Primer extension analysis and functional tests demonstrated the presence of
four new transcriptional start points upstream of the previously reported tts promoter (ttsp). Most interesting,
three of these transcriptional start points are located in a RUP
element thought to be involved in recombinational events (Oggioni,
M. R., and Claverys, J. P. (1999) Microbiology
145, 2647-2653). Transformation experiments using either a recombinant
plasmid containing the whole transcriptional unit of tts or
chromosomal DNA from a type 37 pneumococcus showed that tts
is the only gene required to drive the biosynthesis of a type 37 capsule in S. pneumoniae and other Gram-positive bacteria,
namely Streptococcus oralis, Streptococcus gordonii, and
Bacillus subtilis. The Tts synthase was overproduced in
S. pneumoniae and purified as a membrane-associated enzyme. These membrane preparations used UDP-Glc as substrate to catalyze the
synthesis of a high molecular weight polysaccharide immunologically identical to the type 37 capsule. In addition, UDP-Gal was also a
substrate to produce type 37 polysaccharide since a strong
UDP-Glc-4'-epimerase activity is associated to the membrane fraction of
S. pneumoniae. These results indicated that Tts has a dual
biochemical activity that leads to the synthesis of the branched type
37 polysaccharide.
*
This work was supported in part by Grants PB96-0809 and
BMC2000-1002 from the Dirección General de Investigación
Científica y Técnica.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of a doctoral fellowship from Programa Sectorial de
Formación de Profesorado Universitario y Personal Investigador (Ministerio de Educación y Cultura).
§
To whom correspondence should be addressed. Tel.: 34-91-561-1800;
Fax: 34-91-562-7518; E-mail: e.garcia@cib.csic.es.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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