Two Kunitz-type Proteinase Inhibitors from Potato Tubers

Overview

Journal Plant Physiol

Specialty Physiology

Date 1991 Sep 1

PMID 16668362

Citations 12

Authors

T A Walsh

W P Twitchell

Affiliations

Soon will be listed here.

Abstract

Two proteinase inhibitors have been isolated from tubers of potato (Solanum tuberosum). Based on N-terminal amino acid sequence homologies, they are members of the Kunitz family of proteinase inhibitors. Potato Kunitz inhibitor-1 (molecular weight 19,500, isoelectric point 6.9) is a potent inhibitor of the animal pancreatic proteinase trypsin, and its amino terminus has significant homology to a recently characterized cathepsin D Kunitz inhibitor from potato tubers (Mares et al. [1989] FEBS Lett 251:94-98). Potato Kunitz inhibitor-2 (molecular weight 20,500, isoelectric point 8.6) is an inhibitor of the microbial proteinase subtilisin Carlsberg; its amino terminus is almost identical to an abundant 22 kilodalton protein from potato tubers (Suh et al. [1990] Plant Physiol 94:40-45) and has significant homology to other Kunitz-type subtilisin inhibitors from small grains. Both Kunitz inhibitors are abundant proteins of the cortex of potato tubers.

Citing Articles

Zebra chip disease decreases tuber (Solanum tuberosum L.) protein content by attenuating protease inhibitor levels and increasing protease activities.

Kumar G, Knowles L, Knowles N Planta. 2015; 242(5):1153-66.

PMID: 26092706 DOI: 10.1007/s00425-015-2346-9.

Defense response in non-genomic model species: methyl jasmonate exposure reveals the passion fruit leaves' ability to assemble a cocktail of functionally diversified Kunitz-type trypsin inhibitors and recruit two of them against papain.

Botelho-Junior S, Machado O, Fernandes K, Lemos F, Perdizio V, Oliveira A Planta. 2014; 240(2):345-56.

PMID: 24849173 DOI: 10.1007/s00425-014-2085-3.

The role of the proteinase inhibitor ovorubin in apple snail eggs resembles plant embryo defense against predation.

Dreon M, Ituarte S, Heras H PLoS One. 2010; 5(12):e15059.

PMID: 21151935 PMC: 2997075. DOI: 10.1371/journal.pone.0015059.

A chickpea Kunitz trypsin inhibitor is located in cell wall of elongating seedling organs and vascular tissue.

Jimenez T, Martin I, Labrador E, Dopico B Planta. 2007; 226(1):45-55.

PMID: 17226027 DOI: 10.1007/s00425-006-0465-z.

A novel function for the cathepsin D inhibitor in tomato.

Lison P, Rodrigo I, Conejero V Plant Physiol. 2006; 142(3):1329-39.

PMID: 17012408 PMC: 1630738. DOI: 10.1104/pp.106.086587.

References

Rancour J, Ryan C . Isolation of a carboxypeptidase B inhibitor from potattoes. Arch Biochem Biophys. 1968; 125(1):380-3. DOI: 10.1016/0003-9861(68)90675-9. View

Ritonja A, Krizaj I, Mesko P, Kopitar M, Lucovnik P, Strukelj B . The amino acid sequence of a novel inhibitor of cathepsin D from potato. FEBS Lett. 1990; 267(1):13-5. DOI: 10.1016/0014-5793(90)80275-n. View

Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View

Melville J, Ryan C . Chymotrypsin inhibitor I from potatoes. Large scale preparation and characterization of its subunit components. J Biol Chem. 1972; 247(11):3445-53. View

Kim S, Hara S, Hase S, Ikenaka T, Toda H, Kitamura K . Comparative study on amino acid sequences of Kunitz-type soybean trypsin inhibitors, Tia, Tib, and Tic. J Biochem. 1985; 98(2):435-48. DOI: 10.1093/oxfordjournals.jbchem.a135298. View

Geoffroy P, Legrand M, Fritig B . Isolation and characterization of a proteinaceous inhibitor of microbial proteinases induced during the hypersensitive reaction of tobacco to tobacco mosaic virus. Mol Plant Microbe Interact. 1990; 3(5):327-33. DOI: 10.1094/mpmi-3-327. View

Joubert F, Heussen C, DOWDLE E . The complete amino acid sequence of trypsin inhibitor DE-3 from Erythrina latissima seeds. J Biol Chem. 1985; 260(24):12948-53. View

Yamamoto M, Hara S, Ikenaka T . Amino acid sequences of two trypsin inhibitors from winged bean seeds (Psophocarpus tetragonolobus (L)DC.). J Biochem. 1983; 94(3):849-63. DOI: 10.1093/oxfordjournals.jbchem.a134427. View

Mares M, MELOUN B, Pavlik M, Kostka V, Baudys M . Primary structure of cathepsin D inhibitor from potatoes and its structure relationship to soybean trypsin inhibitor family. FEBS Lett. 1989; 251(1-2):94-8. DOI: 10.1016/0014-5793(89)81435-8. View

10.

Rodis P, Hoff J . Naturally occurring protein crystals in the potato : inhibitor of papain, chymopapain, and ficin. Plant Physiol. 1984; 74(4):907-11. PMC: 1066790. DOI: 10.1104/pp.74.4.907. View

11.

Nozawa H, Yamagata H, Aizono Y, Yoshikawa M, Iwasaki T . The complete amino acid sequence of a subtilisin inhibitor from adzuki beans (Vigna angularis). J Biochem. 1989; 106(6):1003-8. DOI: 10.1093/oxfordjournals.jbchem.a122955. View

12.

Bryant J, Green T, Gurusaddaiah T, Ryan C . Proteinase inhibitor II from potatoes: isolation and characterization of its protomer components. Biochemistry. 1976; 15(16):3418-24. DOI: 10.1021/bi00661a004. View

13.

Rowan A, Brzin J, Buttle D, Barrett A . Inhibition of cysteine proteinases by a protein inhibitor from potato. FEBS Lett. 1990; 269(2):328-30. DOI: 10.1016/0014-5793(90)81186-r. View

14.

Suh S, Peterson J, Stiekema W, Hannapel D . Purification and characterization of the 22-kilodalton potato tuber proteins. Plant Physiol. 1990; 94(1):40-5. PMC: 1077186. DOI: 10.1104/pp.94.1.40. View