Galli G

References (2)

Title : Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae - Tettelin_2002_Proc.Natl.Acad.Sci.U.S.A_99_12391
Author(s) : Tettelin H , Masignani V , Cieslewicz MJ , Eisen JA , Peterson S , Wessels MR , Paulsen IT , Nelson KE , Margarit I , Read TD , Madoff LC , Wolf AM , Beanan MJ , Brinkac LM , Daugherty SC , DeBoy RT , Durkin AS , Kolonay JF , Madupu R , Lewis MR , Radune D , Fedorova NB , Scanlan D , Khouri H , Mulligan S , Carty HA , Cline RT , Van Aken SE , Gill J , Scarselli M , Mora M , Iacobini ET , Brettoni C , Galli G , Mariani M , Vegni F , Maione D , Rinaudo D , Rappuoli R , Telford JL , Kasper DL , Grandi G , Fraser CM
Ref : Proc Natl Acad Sci U S A , 99 :12391 , 2002
Abstract : The 2,160,267 bp genome sequence of Streptococcus agalactiae, the leading cause of bacterial sepsis, pneumonia, and meningitis in neonates in the U.S. and Europe, is predicted to encode 2,175 genes. Genome comparisons among S. agalactiae, Streptococcus pneumoniae, Streptococcus pyogenes, and the other completely sequenced genomes identified genes specific to the streptococci and to S. agalactiae. These in silico analyses, combined with comparative genome hybridization experiments between the sequenced serotype V strain 2603 V/R and 19 S. agalactiae strains from several serotypes using whole-genome microarrays, revealed the genetic heterogeneity among S. agalactiae strains, even of the same serotype, and provided insights into the evolution of virulence mechanisms.
ESTHER : Tettelin_2002_Proc.Natl.Acad.Sci.U.S.A_99_12391
PubMedSearch : Tettelin_2002_Proc.Natl.Acad.Sci.U.S.A_99_12391
PubMedID: 12200547
Gene_locus related to this paper: strag-ESTA , strag-GBS0040 , strag-GBS1828 , strag-pepx , strag-SAG0108 , strag-SAG0246 , strag-SAG0383 , strag-SAG0521 , strag-SAG0679 , strag-SAG0680 , strag-SAG0681 , strag-SAG0785 , strag-SAG0912 , strag-SAG1040 , strag-SAG1562 , strag-SAG2132

Title : Characterization of the syringomycin synthetase gene cluster. A link between prokaryotic and eukaryotic peptide synthetases - Guenzi_1998_J.Biol.Chem_273_32857
Author(s) : Guenzi E , Galli G , Grgurina I , Gross DC , Grandi G
Ref : Journal of Biological Chemistry , 273 :32857 , 1998
Abstract : With this work we have completed the characterization of the syringomycin synthetase gene cluster. In particular, by sequencing additional 28.5 kilobase pairs we show that the nine modules involved in the binding of the nine amino acids of syringomycin are localized on SyrB and SyrE, with SyrE carrying eight modules. The recombinant SyrB and the first and second modules of SyrE (SyrE1 and SyrE2) have been expressed in Escherichia coli and purified. The biochemical data indicate that SyrB binds threonine, the putative precursor of the last amino acid of syringomycin, whereas SyrE1 and SyrE2 bind serine, the first and the second amino acids of syringomycin, respectively. On the basis of the sequence analysis and the biochemical data presented here, it appears that syringomycin synthetase is unique among peptide synthetases in that its genetic organization does not respect the "colinearity rule" according to which the order of the amino acid binding modules along the chromosome parallels the order of the amino acids on the peptide. This feature, together with the absence of a single transcription unit and the absence of epimerase-like domains make syringomycin synthetase more related to the eukaryotic peptide synthetases than to the bacterial counterparts.
ESTHER : Guenzi_1998_J.Biol.Chem_273_32857
PubMedSearch : Guenzi_1998_J.Biol.Chem_273_32857
PubMedID: 9830033
Gene_locus related to this paper: psesy-syrc , psesy-SYRE