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Stress inducible proteinase inhibitor diversity in Capsicum annuum

Manasi Mishra1, Neha Mahajan1, Vaijayanti A Tamhane13, Mahesh J Kulkarni1, Ian T Baldwin2, Vidya S Gupta1 and Ashok P Giri1*

Author Affiliations

1 Plant Molecular Biology Unit, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune, MS, 411 008, India

2 Department of Molecular Ecology, Max Planck Institute for Chemical Ecology, Jena, 07745, Germany

3 Present address: Institute of Bioinformatics and Biotechnology, University of Pune, Pune, MS, 411 007, India

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BMC Plant Biology 2012, 12:217  doi:10.1186/1471-2229-12-217

Published: 16 November 2012

Additional files

Additional file 1:

Table S1. Oligonucleotide primers used for RT-PCR and CanPI internal differentiation. Table S2: Protein identification by MALDI-TOF-MS/MS, database searches.

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Additional file 2:

Figure S1. Multiple sequence alignment of deduced aa sequences of signal peptides (SP-1 to SP-10) of CanPI genes, displaying variations.

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Additional file 3:

Figure S2. Multiple sequence alignment of deduced aa sequences of IRDs (28 in number) constituting all the CanPI genes. The reactive site residue P1 is marked by an arrow. Presence of Lys (K) or Arg (R) at P1 site, indicates trypsin inhibitory site (TI) and Leu (L) indicates chymotrypsin inhibitory site (CI). The core reactive site is marked by an orange box.

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Additional file 4:

Figure S3. Tissue-specific TI activity in various tissues of a mature C. annuum plant. Concentration is represented in terms of trypsin inhibitory units (TIUs/mg). Flower tissue shows the highest TIUs with an almost 7-fold increase compared to leaf tissue. Stem and early fruit tissue also shows significantly higher TI activity.

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