Genetic identification of exported proteins in Streptococcus pneumoniae.

Abstract:

:A strategy was developed to mutate and genetically identify exported proteins in Streptococcus pneumoniae. Vectors were created and used to screen pneumococcal DNA in Escherichia coli and S. pneumoniae for translational gene fusions to alkaline phosphatase (PhoA). Twenty five PhoA+ pneumococcal mutants were isolated and the loci from eight of these mutants showed similarity to known exported or membrane-associated proteins. Homologues were found to: (i) protein-dependent peptide permeases, (ii) penicillin-binding proteins, (iii) Clp proteases, (iv) two-component sensor regulators, (v) the phosphoenolpyruvate: carbohydrate phosphotransferases permeases, (vi) membrane-associated dehydrogenases, (vii) P-type (E1E2-type) cation transport ATPases, (viii) ABC transporters responsible for the translocation of the RTX class of bacterial toxins. Unexpectedly one PhoA+ mutant contained a fusion to a member of the DEAD protein family of ATP-dependent RNA helicases suggesting export of these proteins.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Pearce BJ,Yin YB,Masure HR

doi

10.1111/j.1365-2958.1993.tb01233.x

subject

Has Abstract

pub_date

1993-09-01 00:00:00

pages

1037-50

issue

5

eissn

0950-382X

issn

1365-2958

journal_volume

9

pub_type

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