Proceedings book download - 5Z.com

Vv-AMP1Vv-AMP1...vaearRTCESQSHRFKGTCVRQSNCAAVCQTEGFHGGNCRGFRRRCFCTKHC...mvaeaRTCESQSHRFKGTCVRQSNCAAVCQTEGFHGGNCRGFRRRCFCTKHC100,0%100,0%Vv-AMP2 ...mvaeaRPCESQSPRFKGTCVRQSNCAAVCQTEGFHGGNCRGFRRRCFCTKHC 95,7%Vv-AMP3 ...mvaeaKTCESQSHRFKGTCVRHSNCAAVCQTEGFHGGNCRGFRRRCFCTKHC 95,7%Vv-AMP4 ...meaeaRTCDSQSHRFKGTCVTHINCAAVCHTDGFHGRNCRGFRRPCFCTKHC 83,0%Vv-AMP5 ...qeteaRLCESQSHWFRGVCVSNHNCAVVCRNEHFVGGRCRGFRRRCFCTRNC 68,1%Vv-AMP6 ...vpseaRVCESQSHKFEGACMGDHNCALVCRNEGFSGGKCKGLRRRCFCTKLC 66,0%Fig. 1. Sequence alignment of DEGECHIVID uncharacterized proteins and known grapeantimicrobial oligopeptide Vv-AMP1 (capital letters). Small letters show a part of outsideoligopeptide sequence.Nt-RALFVv-RALF1...rrilATKKYISYGALQKNSVPCSRRGASYYNCKPGAQANPYSRGCSAITRCRS...rrilATSKYISYGALQRNSVPCSRRGASYYNCQPGAQANPYNRGCSTITRCRS100,0%89,8%Vv-RALF2 ...rrilASKRYISYGALSRNSVPCSRRGASYYNCRPGAQANPYTRGCSAITRCRR 85,7%Vv-RALF3 ...rrslAQRRRYISYGALRRNQVPCNRRGRSYYNCRRGGRANPYRRGCSVITKCHRFTD 63,3%Vv-RALF4 ...rrvlVMQKKYISYETLKKDMIPCARPGASYYNCRASGEANPYNRGCEVITGCARGVRDINS 57,1%Fig. 2. Sequence alignment of DEGECHIVID uncharacterized proteins and known tobacco(Nicotiana tabacum) RALF primary structure. RRXL motif is underlined in outsideoligopeptide sequence.It has been pointed out that the mature tobacco RALF oligopeptide was released from itsprecursor by proteolysis [3] because there were specific subtilase site [9] with a dibasicamino acid residue motif RRXL in pro-peptide region of precursor. This motif was foundin all our primary structures. We did not know exactly where precursors of putativeoligopeptides might be split. However, some evidences of predicted sequences exist. Thesame position of dibasic amino acid motif RRXL and oligopeptide in protein and in knownprecursors of plant oligopeptides at the C terminus were these proofs. Nevertheless, theproblem of existence of predicted oligopeptides might be finally solved after their directextraction from the grape followed by sequencing.Functional type of the predicted oligopeptide is usually postulated to be the same typeas of known homologs. However, Figure 2 demonstrates that RALF oligopeptides containmany positively charged residues K or R. This feature is common to a wide variety ofantimicrobial oligopeptides. Such similarity indicates that RALF molecules can potentiallyparticipate in other plant regulatory processes, i.e., to be the polyfunctional regulators.AcknowledgementsOur thanks to H. Peña-Cortes for kindly providing access to DEGECHIVID data. This study wassupported by Chilean National Science and Technology Research Fund FONDECYT, Grant No.1080504.References1. Zamyatnin, A.A. Protein Seq. and Data Anal. 4, 49-52 (1991).2. Zamyatnin, A.A., Borchikov, A.S., et al. Nucl. Acids Res. 34, 261-266 (2006).3. Pearce, G., Morua, D.S., et al. Proc. Natl. Acad Sci. U.S.A. 98, 12843-12847 (2001).4. Zamyatnin, A.A. J. Health Sci. 2, 179-183 (2009).5. Zamyatnin, A.A., Voronina, O.L. Biochem. (Moscow) 75, 214-223 (2010).6. Peña-Cortes, H., Cuadros, A., et al. Abstr. Plant & Animal Genomes IV Conf. W166 (2006).7. de Beer, A., Vivier, M.A. BioMed Central Plant Biol. 8, 75 (2008).8. Zamyatnin. A.A. Recent Adv. Biol. Biophys. Bioeng. Comput. Chem. 5, 33-38 (2009).9. Siezen, R.J., Leunisson, J.A. Protein Sci. 6, 501-523 (1997).413