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Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis
Article first published online: 4 JUL 2008
© 2008 The Authors. Journal compilation © 2008 Blackwell Publishing Ltd
The Plant Journal
Volume 56, Issue 2, pages 219–227, October 2008
How to Cite
Srivastava, R., Liu, J.-X. and Howell, S. H. (2008), Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis. The Plant Journal, 56: 219–227. doi: 10.1111/j.1365-313X.2008.03598.x
- Issue published online: 8 OCT 2008
- Article first published online: 4 JUL 2008
- Received 23 January 2008; revised 1 May 2008; accepted 12 May 2008; published online 1 August 2008.
Figure S1. MS/MS analysis of pAtPSK4-myc. (a) Amino acid sequence of ppAtPSK4-myc is shown in which the signal peptide is underlined, peptide sequences identified by MALDI-TOF are highlighted in red and corresponding mass peaks are indicated. (b) MS/MS spectrum of peptide with mass peak of 974.5 derived from the myc tag. (c) MS/MS spectrum of peptide with mass peak of 576.3 derived from the precursor region of ppAtPSK4-myc. (d) MS/MS spectrum of peptide with mass peak of 690.4 derived from the precursor region of ppAtPSK4-myc.
Figure S2. RT-PCR analysis of AtSBT1.1 transcripts in wt and sbt1.1-1 and -2 mutants. RNA was obtained from 14-day-old seedlings.
Figure S3. pAtPSK4-myc processing is restored in F1 hybrids resulting from an outcross of 35S:ppAtPSK4-myc sbt1.1-1 to wild type. Western blot of extracts from root explants at 0 time or incubated for 1 day on CIM. 35S:ppAtPSK4-myc is expressed in a sbt1.1-1 background or in the F1 of a cross between sbt1.1-1 x wt.
Figure S4. AtSBT1.1-YFP and AtPSK4-YFP are located in the apoplast. Plasmolysis of root cells from transgenic seedlings expressing AtSBT1.1-YFP (a–c) and AtPSK4-YFP (d–f) was carried out by treating root segments with 1 m KNO3 for 10 min. DIC images (a, d) were superimposed on epifluorescent images (b, e) to generate merged images (c, f). Bar = 50 μm.
Figure S5. MS/MS spectrum for the cleaved N-terminal fluorogenic peptide (mass = 862.2). The parent peptide corresponds to residues RRSLVL of which each residue is represented by its b and y ions in the spectrum.
Table S1. Primers used for PCR and qRT-PCR analysis.
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