Siezen RJ, Leunissen JAM: Subtilases: The superfamily of subtilisin-like serine proteases. Prot Sci 6: 501–523(1997).
Google Scholar
Siezen RJ, de Vos WM, Leunissen JAM, Dijkstra BW: Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Prot Enging 4: 719–737(1991).
Google Scholar
Steiner DF, Smeekens SP, Ohagi S, Chan SJ: The new enzymology of precursor processing endoproteases. J Biol Chem 267: 23435–23438(1992).
PubMed
Google Scholar
Seidah NG, Chrétien M, Day R: The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functions. Biochimie 76: 197–209(1994).
Article
PubMed
Google Scholar
Nakayama K: Furin: a mammalian subtilisin/kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem J 327: 625–635(1997).
PubMed
Google Scholar
Barr PJ: Mammalian Subtilisins: The long-sought dibasic processing endoproteases. Cell 66: 1–3(1991).
PubMed
Google Scholar
Schaller A, Ryan CA: Identification of a 50-kDa systeminbinding protein in tomato plasma membranes having Kex2plike properties. Proc Natl Acad Sci USA 91: 11802–11806 (1994).
PubMed
Google Scholar
Kinal H, Park C-M, Berry JO, Koltin Y, Bruenn JA: Processing and secretion of a virally encoded antifungal toxin in transgenic tobacco plants: evidence for a kex2p pathway in plants. Plant Cell 7: 677–688(1995).
PubMed
Google Scholar
Yamagata H, Masuzawa T, Nagaoka Y, Ohnishi T, Iwasaki T: cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a large precursor. J Biol Chem 269: 32725–32731(1994).
PubMed
Google Scholar
Ribeiro A, Akkermans ADL, van Kammen A, Bisseling T, Pawlowski K: A nodule-specific gene encoding a subtilisinlike protease is expressed in early stages of actinorhizal nodule development. Plant Cell 7: 785–794(1995).
PubMed
Google Scholar
Taylor AA, Horsch A, Rzepczyk A, Hasenkampf CA, Riggs CD: Maturation and secretion of a serine proteinase is as sociated with events of late microsporogenesis. Plant J 12: 1261–1271(1997).
PubMed
Google Scholar
Tornero P, Conejero V, Vera P: Primary structure and expression of a pathogen-induced protease (PR-P69) in tomato plants: similarity of functional domains to subtilisin-like endoproteases. Proc Natl Acad Sci USA 93: 6332–6337(1996).
PubMed
Google Scholar
Thornero P, Conejero V, Vera P: Identification of a new pathogen-induced member of the subtilisin-like protease family from plants. J Biol Chem 272: 14412–14419(1997).
PubMed
Google Scholar
Riggs CD, Horsch A: Molecular cloning of an anther specific gene from tomato. Plant Physiol 108: 117 (1995).
Google Scholar
Uchikoba T, Yonezawa H, Kaneda M: Cleavage specificity of cucumisin, a plant serine protease. J Biochem 117: 1126–1130 (1995).
PubMed
Google Scholar
Yonezawa H, Uchikoba T, Kaneda M: Identification of the reactive histidine of cucumisin, a plant serine protease: modification with chloromethyl ketone derivative of peptide substrate. J Biochem 118: 917–920(1995).
PubMed
Google Scholar
Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1989).
Google Scholar
Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K: Current Protocols in Molecular Biology. Greene Publishing Associates/Wiley-Interscience, New York (1987).
Google Scholar
Heitz T, Bergey DR, Ryan CA: A gene encoding a chloroplasttargeted lipoxygenase in tomato leaves is transiently induced by wounding, systemin, and methyl jasmonate. Plant Physiol 114: 1085–1093(1997).
PubMed
Google Scholar
Genetics Computer Group: Program Manual for the Wisconsin Package, Vers. 8.0. GCG, Madison, WI (1994).
Google Scholar
Murray MG, Thompson WF: Rapid isolation of high molecular weight plant DNA. Nucl Acids Res 8: 4321–4325 (1980).
PubMed
Google Scholar
Vera P, Conejero V: Pathogenesis-related proteins of tomato. P-69 as an alkaline endoproteinase. Plant Physiol 87: 58–63 (1988).
Google Scholar
Royo J, Nass N, Matton DP, Okamoto S, Clarke AE, Newbigin E: A retrotransposon-like sequence linked to the S-locus of Nicotiana alata is expressed in styles in response to touch. Mol Gen Genet 250: 180–188(1996).
PubMed
Google Scholar
Ujwal S, Masayori I: Propeptide-mediated folding in subtilisin: the intramolecular chaperone concept. In: Richard B, Christian B (eds) Subtilisin Enzymes: Practical Protein Engineering, Vol. 379, pp. 147–154. Plenum Press, New York (1996).
Google Scholar
Siezen RJ, Leunissen JAM, Shinde U: Homology analysis of the propeptides of subtilisin-like serine proteases (subtilases). In: Shinde U (ed) Intramolecular Chaperones and Folding, pp. 231–253. R. G. Landes Company, Austin, TX (1995).
Google Scholar
Creemers JWM, Jackson RS, Hutton JC: Molecular and cellular regulation of prohormone processing. Sem Cell Dev Biol 9: 3–10(1998).
Google Scholar
Gensberg K, Shamem J, Matthews GM: Subtilisin-related serine proteases in the mammalian constitutive secretory pathway. Sem Cell Dev Biol 9: 11–17(1998).
Google Scholar
Tornero P, Mayda E, Gó mez MD, Canas L, Conejero V, Vera P: Characterization of LRP, a leucine-rich repeat (LRR) protein from tomato plants that is processed during pathogenesis. Plant J 10: 315–330(1996).
PubMed
Google Scholar
Shinde U, Li Y, Inouye M: Propeptide mediated protein folding: intramolecular chaperones. In: Shinde U, Inouye M (eds) Intramolecular Chaperones and Protein Folding, pp. 1–9. R.G. Landes Company, Austin, TX (1995).
Google Scholar
Eder J, Rheinnecker M, Fersht A: The pro-sequence assists subtilisin BPN to fold from an intermediate to the native state: a common mechanism for proteases, but not for all proteins with pro-sequences. In: Shinde U, Inouye M (eds) Intramolecular Chaperones and Protein Folding, pp. 35–60. R.G. Landes Company, Austin, TX (1995).
Google Scholar
Thomas G, Molloy SS, Anderson ED, Thomas L: Multi-step activation of furin: a model for the eukaryotic proprotein convertases. In: Shinde U, Inouye M (eds) Intramolecular Chaperones and Protein Folding, pp. 157–179. R.G. Landes Company, Austin, TX (1995).
Google Scholar
Shennan KIJ, Taylor NA, Jermany JL, Matthews G, Docherty K: Differences in pH optima and calcium requirements for maturation of the prohormone convertases PC2 and PC3 indicates different intracellular locations for these events. J Biol Chem 270: 1402–1497(1995).
PubMed
Google Scholar
Bevan M, Bancroft I, Bent E, Love K, Goodman H, Dean C, Bergkamp R, Dirkse W, van Staveren M, Stiekema W et al.: Analysis of 1.9Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana. Nature 391: 485–488(1998).
PubMed
Google Scholar
Gilbert W, Marchionni M, McKnight G: On the antiquity of introns. Cell 46: 151–154(1986).
Article
PubMed
Google Scholar
Rose AB, Last RL: Introns act post-transcriptionally to increase expression of the Arabidopsis thaliana tryptophan pathway gene PAT1. Plant J 11: 455–464(1997).
PubMed
Google Scholar
Corpet F: Multiple sequence alignment with hierarchical clustering. Nucl Acids Res 16: 10881–10890(1988).
PubMed
Google Scholar
Benner SA, Badcoe I, Cohen MA, Gerloff DL: Bona fide prediction of aspects of protein conformation. Assigning interior and surface residues from patterns of variation and conservation in homologous protein sequences. J Mol Biol 235: 926–958(1994).
PubMed
Google Scholar