Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
OXYGEN SENSITIVITY AND METAL ION-DEPENDENT TRANSCRIPTIONAL ACTIVATIONBY NIFA PROTEIN FROM RHIZOBIUM-LEGUMINOSARUM BIOVAR TRIFOLII
Autore:
SCREEN S; WATSON J; DIXON R;
Indirizzi:
UNIV SUSSEX,AFRC,INST PLANT SCI RES,NITROGEN FIXAT LAB BRIGHTON BN1 9RQ E SUSSEX ENGLAND UNIV SUSSEX,AFRC,INST PLANT SCI RES,NITROGEN FIXAT LAB BRIGHTON BN1 9RQ E SUSSEX ENGLAND CSIRO,DIV PLANT IND CANBERRA ACT 2601 AUSTRALIA
Titolo Testata:
MGG. Molecular & general genetics
fascicolo: 3, volume: 245, anno: 1994,
pagine: 313 - 322
SICI:
0026-8925(1994)245:3<313:OSAMIT>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
MULTICOPY EXPRESSION VECTORS; NITROGEN-FIXATION GENES; KLEBSIELLA-PNEUMONIAE; ESCHERICHIA-COLI; MELILOTI-NIFA; POSITIVE CONTROL; REGULATORY PROTEINS; BETA-GALACTOSIDASE; CYSTEINE RESIDUES; OVER-PRODUCTION;
Keywords:
NITROGEN FIXATION; NIFA; METAL IONS; OXYGEN REGULATION; TRANSCRIPTIONAL ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
S. Screen et al., "OXYGEN SENSITIVITY AND METAL ION-DEPENDENT TRANSCRIPTIONAL ACTIVATIONBY NIFA PROTEIN FROM RHIZOBIUM-LEGUMINOSARUM BIOVAR TRIFOLII", MGG. Molecular & general genetics, 245(3), 1994, pp. 313-322

Abstract

The NIFA protein from Rhizobium leguminosarum biovar trifolii (R. trifolii) strain ANU843 lacks an N-terminal domain present in homologous NIFA proteins from other diazotrophs. The R. trifolii nifA gene product is unstable when expressed in Escherichia coli under both aerobic and microaerobic conditions. Stability is increased by fusion of additional amino acids to the N-terminus of the protein or by expression of nifA in sno mutant (presumed protease deficient) strains of E. coli. Transcriptional activation in vivo by R. trifolii NIFA decreases under aerobic growth conditions, or when cultures are depleted of metal ions. In sno mutant strains this decrease in activity reflects a loss of specific activity rather than proteolytic degradation, implying that R. trifolii NIFA requires metal ions for activity and is oxygen sensitive. The addition of 30 amino acids to the amino-terminus of R. trifolii NIFA results in an oxygen-tolerant protein, with metal ion-dependent activity. Metal ions are therefore not only required for oxygen sensingby R. trifolii NIFA but may play an additional role in determining NIFA structure or activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 23:41:07