Abstract:
:VMA1 translational product undergoes excision of a 50-kDa intervening segment (VDE: VMA1-derived endonuclease) and religation of the flanking regions to create a 69-kDa catalytic subunit of vacuolar membrane H+-ATPase. VDEs conjugated with polypeptides at both N- and C-terminal ends were expressed in Escherichia coli and examined for their ability to catalyze self-splicing. Processed VDE was found in soluble pools, while unspliced precursors accumulated in insoluble pools, forming inclusion bodies. We demonstrate in vitro protein splicing by refolding of the denatured precursor molecules. The processing reaction efficiently occurs with the purified precursor peptide. VDE bracketed by only 6 proximal and 4 distal amino acids is autocatalytically processed.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Kawasaki M,Makino S,Matsuzawa H,Satow Y,Ohya Y,Anraku Ydoi
10.1006/bbrc.1996.0826subject
Has Abstractpub_date
1996-05-24 00:00:00pages
827-32issue
3eissn
0006-291Xissn
1090-2104pii
S0006291X96908268journal_volume
222pub_type
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