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Genetic resistances to plant viruses and their vectors

Bibliographic Reference from IPV
Plant/Virus Interactions - UMR GDPP - Research Centre INRA Bordeaux-Aquitaine - INRA
Villenave d'Ornon - France

More data about this group.

Last database update for these data: 2008-06-04 - Data extracted on 2009-04-14 from the database.

Biochemical identification of proteasome-associated endonuclease activity in sunflower

Bibliographic Reference
Field Value
Document typeJournal article: paper
LanguageEnglish
Year2003
AuthorsBallut, L.
Petit, F.
Mouzeyar, S.
Le Gall, O.
Candresse, T.
Schmid, P.
Nicolas, P.
Badaoui, S.
TitleBiochemical identification of proteasome-associated endonuclease activity in sunflower
SourceBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume1645
Issue1
Pages30-39
AbstractProteasomes have been purified from sunflower hypocotyles. They elute with a molecular mass of 600 kDa from gel filtration columns and two-dimensional gel electrophoresis indicates that the complex contains at least 20 different protein subunits. Peptide microsequencing revealed the presence of four subunits homologous to subunits Beta2, Beta6, Alpha5 and Alpha6 of plant proteasomes. These proteasomes have chymotrypsin-like activity and the highly purified fraction of this complex is associated with an endonuclease activity hydrolyzing Tobacco mosaic virus RNA and Lettuce mosaic virus RNA with a cleavage pattern showing fragments of well-defined size. This is the first evidence of a RNA endonuclease activity associated with plant proteasomes.
Web pageWeb page Pubmed
DescriptorsAmino Acid Sequence
Chromatography Gel
Chymotrypsin
Cysteine Endopeptidases
Two-Dimensional Gel Electrophoresis
Endonucleases
Endoribonucleases
Helianthus
Molecular Sequence Data
Multienzyme Complexes
Sequence Alignment