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Wyświetlanie 1-2 z 2
Tytuł:
Mass spectrometry identification of membrane-bound respiratory nitrate reductase from Bradyrhizobium sp. (Lupinus)
Autorzy:
Polcyn, Władysław
Powiązania:
https://bibliotekanauki.pl/articles/1040683.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
immunoblot screening
membrane-bound nitrate reductase [EC 1.7.99.4]
enzyme purification
Bradyrhizobium sp. (Lupinus)
rhizobia
mass spectrometry sequencing
Opis:
Respiratory nitrate reductase (NR) from Bradyrhizobium sp. (Lupinus) USDA 3045 has biochemical properties of the membrane-bound NR type. However, in the completely sequenced rhizobium genomes only genes for the periplasmic type of dissimilatory NR were found. Therefore purification and identification of the enzyme by tandem mass spectrometry (MS/MS) was undertaken. MS/MS spectra representing 149 unique tryptic peptides derived from purified 137-kDa subunit matched the NCBInr-deposited NarG sequences. MS/MS sequencing of two other SDS/PAGE bands (65- and 59-kDa) identified them as derivatives of the NarH-type protein. Applying additional validation criteria, 73% of the sequence of the NarG subunit (902 aa) and 52% of NarH sequence (266 aa) was assembled (UniProt KB acc. no. P85097 and P85098). This is the first unambiguous identification of an active NarGH-like NR in rhizobia. Moreover, arguments are provided here for the existence of a functional enzyme of this type also among other rhizobial species, basing on immunoblot screening and the presence of membrane-associated NR-active electrophoretic forms.
Źródło:
Acta Biochimica Polonica; 2008, 55, 4; 753-760
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Nitrate-related down-regulation of respiratory nitrate reductase from Bradyrhizobium sp. (Lupinus)
Autorzy:
Polcyn, Władysław
Powiązania:
https://bibliotekanauki.pl/articles/1040684.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
multiple enzyme forms
membrane-bound nitrate reductase [EC 1.7.99.4]
down-regulation
nitrate and nitrite induction
stability of subunits
Bradyrhizobium sp. (Lupinus)
Opis:
Previously, we showed that anaerobic induction of respiratory nitrate reductase (NR) activity in Bradyrhizobium sp. (Lupinus) USDA 3045 is strongly enhanced by nitrate or nitrite through de novo synthesis. Here, multiple NR-active soluble forms, ranging from 75 kDa to 190 kDa, were observed under anaerobic conditions. Electrophoretic activity band patterns differed depending on the level and the type of the N oxyanion added. The intensity of the membrane-bound NR activity band of 230 kDa changed with time along with consumption of 2 mM nitrate. It was associated with a parallel 5-fold increase and then 2-fold reduction in the amount of membrane-bound NR protein. In contrast, on 4 mM nitrate, the level of NR protein was much more stable, apparently due to slower nitrate depletion. Moreover, in cells anaerobically grown without nitrate addition, a 42-kDa derivative of NR degradation was immunodetected, which was not observed if nitrate was present in the medium. These findings suggest that the amount of the respiratory NR protein could be negatively regulated by endogenous proteases in relation to the level of nitrate available. It seems, therefore, that multiple native forms might be not different isoenzymes but immature complexes or derivatives of the enzyme protein turnover. This report adds to a modest list of bacterial enzymes apparently regulated by proteolysis, such as GS, MurAA, EnvA, GdhA, and MetA.
Źródło:
Acta Biochimica Polonica; 2008, 55, 4; 761-766
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
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