Bertolini MC

References (3)

Title : Comparison of the genomes of two Xanthomonas pathogens with differing host specificities - da Silva_2002_Nature_417_459
Author(s) : da Silva ACR , Ferro JA , Reinach FC , Farah CS , Furlan LR , Quaggio RB , Monteiro-Vitorello CB , Van Sluys MA , Almeida Jr NF , Alves LMC , do Amaral AM , Bertolini MC , Camargo LEA , Camarotte G , Cannavan F , Cardozo J , Chambergo F , Ciapina LP , Cicarelli RMB , Coutinho LL , Cursino-Santos JR , El-Dorry H , Faria JB , Ferreira AJS , Ferreira RCC , Ferro MIT , Formighieri EF , Franco MC , Greggio CC , Gruber A , Katsuyama AM , Kishi LT , Leite JrRP , Lemos EGM , Lemos MVF , Locali EC , Machado MA , Madeira AMBN , Martinez-Rossi NM , Martins EC , Meidanis J , Menck CFM , Miyaki CY , Moon DH , Moreira LM , Novo MTM , Okura VK , Oliveira MC , Oliveira VR , Pereira Jr HA , Rossi A , Sena JAD , Silva C , de Souza RF , Spinola LAF , Takita MA , Tamura RE , Teixeira EC , Tezza RID , Trindade dos Santos M , Truffi D , Tsai SM , White FF , Setubal JC , Kitajima JP
Ref : Nature , 417 :459 , 2002
Abstract : The genus Xanthomonas is a diverse and economically important group of bacterial phytopathogens, belonging to the gamma-subdivision of the Proteobacteria. Xanthomonas axonopodis pv. citri (Xac) causes citrus canker, which affects most commercial citrus cultivars, resulting in significant losses worldwide. Symptoms include canker lesions, leading to abscission of fruit and leaves and general tree decline. Xanthomonas campestris pv. campestris (Xcc) causes black rot, which affects crucifers such as Brassica and Arabidopsis. Symptoms include marginal leaf chlorosis and darkening of vascular tissue, accompanied by extensive wilting and necrosis. Xanthomonas campestris pv. campestris is grown commercially to produce the exopolysaccharide xanthan gum, which is used as a viscosifying and stabilizing agent in many industries. Here we report and compare the complete genome sequences of Xac and Xcc. Their distinct disease phenotypes and host ranges belie a high degree of similarity at the genomic level. More than 80% of genes are shared, and gene order is conserved along most of their respective chromosomes. We identified several groups of strain-specific genes, and on the basis of these groups we propose mechanisms that may explain the differing host specificities and pathogenic processes.
ESTHER : da Silva_2002_Nature_417_459
PubMedSearch : da Silva_2002_Nature_417_459
PubMedID: 12024217
Gene_locus related to this paper: xanac-q8phx9 , xanac-q8pmm6 , xanax-ACVB , xanax-BIOH , xanax-CATD , xanax-CPO , xanax-DHAA , xancp-OleB , xanax-ENTF2 , xanax-estA1 , xanax-GAA , xanax-META , xanax-METX , xanax-PCAD , xanax-PHBC , xanax-PTRB , xanax-Q8PMQ8 , xanax-Q8PQP0 , xanax-XAC0198 , xanax-XAC0262 , xanax-XAC0279 , xanax-XAC0319 , xanax-XAC0372 , xanax-XAC0375 , xanax-XAC0501 , xanax-XAC0515 , xanax-XAC0574 , xanax-XAC0591 , xanax-XAC0619 , xanax-XAC0628 , xanax-XAC0736 , xanax-XAC0753 , xanax-XAC0805 , xanax-XAC0874 , xanax-XAC0916 , xanax-XAC1200 , xanax-XAC1213 , xanax-XAC1591 , xanax-XAC1713 , xanax-XAC1752 , xanax-XAC2126 , xanax-XAC2393 , xanax-XAC2532 , xanax-XAC2541 , xanax-XAC2907 , xanax-XAC2981 , xanax-XAC2987 , xanax-XAC2990 , xanax-XAC3037 , xanax-XAC3053 , xanax-XAC3152 , xanax-XAC3173 , xanax-XAC3315 , xanax-XAC3371 , xanax-XAC3619 , xanax-XAC3674 , xanax-XAC3770 , xanax-XAC3967 , xanax-XAC3999 , xanax-XAC4046 , xanax-XAC4055 , xanax-XAC4106 , xanax-XAC4221 , xanax-XAC4316 , xanax-XYNB , xanca-acvB , xanca-BIOH , xanca-CATD , xanca-CPO , xanca-estA1 , xanca-impep , xanca-META , xanca-METX , xanca-PCAD , xanca-PHBC , xanca-Q8PB04 , xanca-W78 , xanca-XCC0080 , xanca-XCC0180 , xanca-XCC0243 , xanca-XCC0260 , xanca-XCC0266 , xanca-XCC0372 , xanca-XCC0375 , xanca-XCC0753 , xanca-XCC0757 , xanca-XCC0800 , xanca-XCC0843 , xanca-XCC1105 , xanca-XCC1541 , xanca-XCC1734 , xanca-XCC2285 , xanca-XCC2374 , xanca-XCC2397 , xanca-XCC2405 , xanca-XCC2566 , xanca-XCC2722 , xanca-XCC2737 , xanca-XCC2811 , xanca-XCC2817 , xanca-XCC2854 , xanca-XCC2869 , xanca-XCC2957 , xanca-XCC3028 , xanca-XCC3164 , xanca-XCC3219 , xanca-XCC3296 , xanca-XCC3300 , xanca-XCC3308 , xanca-XCC3320 , xanca-XCC3514 , xanca-XCC3548 , xanca-XCC3555 , xanca-XCC3623 , xanca-XCC3885 , xanca-XCC3915 , xanca-XCC3961 , xanca-XCC3970 , xanca-XCC4016 , xanca-XCC4096 , xanca-XCC4180 , xanca-XYNB , xanca-XYNB2 , xancb-b0rq23 , xancp-q8pax3 , xancp-y2094

Title : Expression and characterization of Geotrichum candidum lipase I gene. Comparison of specificity profile with lipase II - Bertolini_1995_Eur.J.Biochem_228_863
Author(s) : Bertolini MC , Schrag JD , Cygler M , Ziomek E , Thomas DY , Vernet T
Ref : European Journal of Biochemistry , 228 :863 , 1995
Abstract : Despite tremendous progress in the elucidation of three-dimensional structures of lipases, the molecular basis for their observed substrate preference is not well understood. In an effort to correlate the lipase structure with its substrate preference and to clarify the contradicting reports in the literature, we have compared the enzymic characteristics of two closely related recombinant lipases from the fungus Geotrichum candidum. These enzymes were expressed in the yeast Saccharomyces cerevisiae as fusions with an N-terminal poly(His) tag and were purified in a single step by metal-affinity chromatography. Their specific activities against a series of triacylglycerol substrates were compared using a titrimetric assay. The substrates varied in fatty acyl chain length, number of double bonds and their position along the chain. G. candidum lipases I and II (GCL I and GLC II) are markedly different with respect to their substrate preferences. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15), GCL I showed higher specific activity than GCL II, whereas GCL II showed higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14). We have constructed a hybrid molecule containing the N-terminal portion of GCL I (including the flap covering the active site) linked to the C-terminal portion of GCL II. The hybrid molecule showed a substrate preference pattern identical to that of GCL II. These results indicate that sequence variation within the N-terminal 194 amino acids of G. candidum lipases do not contribute to the observed variation in efficiency by which the lipases hydrolyze their substrates. Moreover, it also shows that the flap region in GCL is not directly involved in substrate differentiation, even though this region is thought to be involved in recognition of the interface and in the activation of the enzyme.
ESTHER : Bertolini_1995_Eur.J.Biochem_228_863
PubMedSearch : Bertolini_1995_Eur.J.Biochem_228_863
PubMedID: 7737187
Gene_locus related to this paper: geoca-1lipa , geoca-2lipa

Title : Polymorphism in the lipase genes of Geotrichum candidum strains - Bertolini_1994_Eur.J.Biochem_219_119
Author(s) : Bertolini MC , Laramee L , Thomas DY , Cygler M , Schrag JD , Vernet T
Ref : European Journal of Biochemistry , 219 :119 , 1994
Abstract : The fungus Geotrichum candidum produces extracellular lipases. Purification and characterization of different lipase isoforms from various G. candidum strains is difficult due to the close physical and biochemical properties of the isoforms. Consequently, the characterization of these enzymes and their substrate specificities has been difficult. We have determined the lipase genes present in four strains of G. candidum (ATCC 34614, NRCC 205002, NRRL Y-552 and NRRL Y-553) by molecular cloning and DNA sequencing. Each strain contains two genes similar to the previously identified lipase I and lipase II cDNAs. Our data suggest that no other related lipase genes are present in these strains. Each lipase-gene family shows sequence variation (polymorphism) that is confirmed by Southern-blot analysis. This polymorphism and the sequence differences between lipase I and lipase II have been localized within the previously determined three-dimensional structure of lipase II. Although most of the amino acid substitutions are located on the protein surface, some are present in structural features possibly involved in determining substrate specificity.
ESTHER : Bertolini_1994_Eur.J.Biochem_219_119
PubMedSearch : Bertolini_1994_Eur.J.Biochem_219_119
PubMedID: 8306978
Gene_locus related to this paper: geoca-1lipa , geoca-2lipa