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Titolo:
TETRAPAC (TPC), A NOVEL GENOTYPE OF NEISSERIA-GONORRHOEAE AFFECTING EPITHELIAL-CELL INVASION, NATURAL TRANSFORMATION COMPETENCE AND CELL-SEPARATION
Autore:
FUSSENEGGER M; KAHRS AF; FACIUS D; MEYER TF;
Indirizzi:
MAX PLANCK INST BIOL,INFEKT BIOL ABT,SPEMANNSTR 34 D-72076 TUBINGEN GERMANY MAX PLANCK INST BIOL,INFEKT BIOL ABT D-72076 TUBINGEN GERMANY
Titolo Testata:
Molecular microbiology
fascicolo: 6, volume: 19, anno: 1996,
pagine: 1357 - 1372
SICI:
0950-382X(1996)19:6<1357:T(ANGO>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
PILUS ANTIGENIC VARIATION; BACILLUS-SUBTILIS 168; ESCHERICHIA-COLI; CHROMOSOMAL REARRANGEMENT; DEFICIENT MUTANTS; GENE CONVERSION; PHASE VARIATION; RNA-POLYMERASE; CLONED GENES; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
73
Recensione:
Indirizzi per estratti:
Citazione:
M. Fussenegger et al., "TETRAPAC (TPC), A NOVEL GENOTYPE OF NEISSERIA-GONORRHOEAE AFFECTING EPITHELIAL-CELL INVASION, NATURAL TRANSFORMATION COMPETENCE AND CELL-SEPARATION", Molecular microbiology, 19(6), 1996, pp. 1357-1372

Abstract

We characterized a novel mutant phenotype (tetrapac, tpc) of Neisseria gonorrhoeae(Ngo) associated with a distinctive rough-colony morphology and bacterial growth in clusters of four, This phenotype, suggesting a defect in cell division, was isolated from a mutant library of NgoMS11 generated with the phoA mini-transposon TnMax4, The tpc mutant shows a 30% reduction in the overall murein hydrolase activity using Escherichia coli murein as substrate. Tetrapacs can be resolved by co-cultivation with wild-type Ngo, indicating that Tpc is a diffusible protein, Interestingly, Tpc is absolutely required for the natural transformation competence of piliated Ngo. Mutants in tpc grow normally, but show a similar to 10-fold reduction in their ability to invade human epithelial cells. The tpc sequence reveals an open reading frame of similar to 1kb encoding a protein (Tpc) of 37 kDa, The primary gene product exhibits an N-terminal leader sequence typical of lipoproteins, butpalmitoylation of Tpc could not be demonstrated, The ribosomal binding site of tpc is immediately downstream of the translational stop codon of the folC gene coding for an enzyme involved in folic acid biosynthesis and one-carbon metabolism. The tpc gene is probably co-transcribed from the folC promoter and a promoter located within the folC gene. The latter promoter sequence shares significant homology with E. coligearbox consensus promoters. All three mutant phenotypes, i,e. the cell separation defect, the transformation deficiency and the defect in cell invasion can be restored by complementation of the mutant with anintact tpc gene. To some extent the tcp phenotype is reminiscent of lap in Listeria, lytA in Streptococcus pneumoniae and lyt in Bacillus subtilis, all of which are considered to represent murein hydrolase defects.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 22:12:06