Consulta: creatorFacets:"Huergo,L.F."
Registros recuperados: 4
Data/hora: 06/06/2024 02:12:42

Induction of a gloverin-like antimicrobial polypeptide in the sugarcane borer Diatraea saccharalis challenged by septic injury
Provedor de dados: 56
Autores: Silva,J.L.C.; Barbosa,J.F.; Bravo,J.P.; Souza,E.M. de; Huergo,L.F.; Pedrosa,F.O.; Esteves,E.; Daffre,S.; Fernandez,M.A.
Diatraea saccharalis (Fabricius, 1794) (Lepidoptera: Crambidae) is an important pest for Brazilian sugarcane. In the present study, we detected two distinct spots in hemolymph from septic injured larvae (HDs1 and HDs2), which are separated by 2DE gel electrophoresis. Both spots were subjected to in-gel tryptic digestion and MALDI-TOF/TOF analysis, which revealed the sequence VFGTLGSDDSGLFGK present in both HDs1 and HDs2. This sequence had homology and 80% identity with specific Lepidoptera antimicrobial peptides called gloverins. Analyses using the ImageMaster 2D software showed pI 8.94 of the HDs1 spot, which is similar to that described to Hyalophora gloveri gloverin (pI 8.5). Moreover, the 14-kDa molecular mass of the spot HDs1 is compatible to that of...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Diatraea saccharalis; Lepidoptera; Immune response; Gloverin; Sugarcane borer; Hemolymph.
Ano: 2010
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2010000500003

Effect of ATP and 2-oxoglutarate on the in vitro interaction between the NifA GAF domain and the GlnB protein of Azospirillum brasilense
Provedor de dados: 56
Autores: Sotomaior,P.; Araújo,L.M.; Nishikawa,C.Y.; Huergo,L.F.; Monteiro,R.A.; Pedrosa,F.O.; Chubatsu,L.S.; Souza,E.M.
Azospirillum brasilense is a diazotroph that associates with important agricultural crops and thus has potential to be a nitrogen biofertilizer. The A. brasilense transcription regulator NifA, which seems to be constitutively expressed, activates the transcription of nitrogen fixation genes. It has been suggested that the nitrogen status-signaling protein GlnB regulates NifA activity by direct interaction with the NifA N-terminal GAF domain, preventing the inhibitory effect of this domain under conditions of nitrogen fixation. In the present study, we show that an N-terminal truncated form of NifA no longer required GlnB for activity and lost regulation by ammonium. On the other hand, in trans co-expression of the N-terminal GAF domain inhibited the...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Azospirillum brasilense; NifA protein; GlnB protein; GAF domain; Nitrogen fixation.
Ano: 2012
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2012001200005

Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein
Provedor de dados: 56
Autores: Araújo,L.M.; Huergo,L.F.; Invitti,A.L.; Gimenes,C.I.; Bonatto,A.C.; Monteiro,R.A.; Souza,E.M.; Pedrosa,F.O.; Chubatsu,L.S.
Azospirillum brasilense is a diazotroph found in association with important agricultural crops. In this organism, the regulation of nitrogen fixation by ammonium ions involves several proteins including the uridylyltransferase/uridylyl-removing enzyme, GlnD, which reversibly uridylylates the two PII proteins, GlnB and GlnZ, in response to the concentration of ammonium ions. In the present study, the uridylylation/deuridylylation cycle of A. brasilense GlnB and GlnZ proteins by GlnD was reconstituted in vitro using the purified proteins. The uridylylation assay was analyzed using non-denaturing polyacrylamide gel electrophoresis and fluorescent protein detection. Our results show that the purified A. brasilense GlnB and GlnZ proteins were uridylylated by...
Tipo: Info:eu-repo/semantics/other
Palavras-chave: Azospirillum brasilense; Nitrogen fixation; PII-like protein; GlnD; GlnB; GlnZ.
Ano: 2008
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008000400006

A broad pH range and processive chitinase from a metagenome library
Provedor de dados: 56
Autores: Thimoteo,S.S.; Glogauer,A.; Faoro,H.; de Souza,E.M.; Huergo,L.F.; Moerschbacher,B.M.; Pedrosa,F.O.
Chitinases are hydrolases that degrade chitin, a polymer of N-acetylglucosamine linked β(1-4) present in the exoskeleton of crustaceans, insects, nematodes and fungal cell walls. A metagenome fosmid library from a wastewater-contaminated soil was functionally screened for chitinase activity leading to the isolation and identification of a chitinase gene named metachi18A. The metachi18A gene was subcloned and overexpressed in Escherichia coli BL21 and the MetaChi18A chitinase was purified by affinity chromatography as a 6xHis-tagged fusion protein. The MetaChi18A enzyme is a 92-kDa protein with a conserved active site domain of glycosyl hydrolases family 18. It hydrolyses colloidal chitin with an optimum pH of 5 and temperature of 50°C. Moreover, the enzyme...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Chitinase; Metagenomic; Aeromonas; Kinetics.
Ano: 2017
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2017000100602