Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
REDOX MODULATION OF THE EXPRESSION OF BACTERIAL GENES ENCODING CYSTEINE-RICH PROTEINS IN PLANT-PROTOPLASTS
Autore:
PINEIRO M; GARCIAOLMEDO F; DIAZ I;
Indirizzi:
UNIV POLITECN MADRID,ESCUELA TECN SUPER INGN AGRON,BIOQUIM & BIOL MOLEC LAB E-28040 MADRID SPAIN UNIV POLITECN MADRID,ESCUELA TECN SUPER INGN AGRON,BIOQUIM & BIOL MOLEC LAB E-28040 MADRID SPAIN
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 9, volume: 91, anno: 1994,
pagine: 3867 - 3871
SICI:
0027-8424(1994)91:9<3867:RMOTEO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
DISULFIDE BOND FORMATION; ENDOPLASMIC-RETICULUM; SECRETION; CELLS;
Keywords:
THIOLS; DITHIOTHREITOL; NEOMYCIN PHOSPHOTRANSFERASE; BETA-GLUCURONIDASE; THIONIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
M. Pineiro et al., "REDOX MODULATION OF THE EXPRESSION OF BACTERIAL GENES ENCODING CYSTEINE-RICH PROTEINS IN PLANT-PROTOPLASTS", Proceedings of the National Academy of Sciences of the United Statesof America, 91(9), 1994, pp. 3867-3871

Abstract

Activity of neomycin phosphotransferase II (NPTII; gene, neo; five cysteines) in tobacco protoplasts transfected with fusions of the octopine TR2' or cauliflower mosaic virus 35S promoter and the nea gene, with or without a signal peptide, increased up to 8-fold in response to externally added dithiothreitol at concentrations that did not affect protoplast viability (up to 2.5 mM). Activity of phosphinothricin acetyltransferase (PAT; gene, bar; one cysteine) expressed under control ofthe TR1' or 35S promoter was not similarly affected, thus excluding aredox modulation of transcription as the mechanism of NPTII activation by dithiothreitol. Western blot analyses showed an increase in the amount bf protein in response to dithiothreitol, whereas neither the steady-state level of NPTII mRNA nor the specific activity of the purified enzyme was affected. The same type of modulation was observed for transiently expressed beta-glucuronidase (nine cysteines) produced froma fusion with the 35S promoter, with or without a signal peptide. Limitation of cotranslational and/or early posttranslational steps by excessively oxidizing sulfhydryl/disulfide redox potentials is postulatedto explain the low net accumulation of cysteine-rich proteins of bacterial origin (i.e.; NPTII and beta-glucuronidase) when expressed in plant protoplasts, and the marked increase in such proteins in response to externally added dithiothreitol.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 12:21:11