Hostname: page-component-78c5997874-ndw9j Total loading time: 0 Render date: 2024-11-11T05:52:30.467Z Has data issue: false hasContentIssue false
  • English
  • Français

Cloning and nucleotide sequence of the cDNA encoding a β-1,3-glucanase-like protein secreted from growing pollen tubes of Japanese pear (Pyrus pyrifolia)

Published online by Cambridge University Press:  12 February 2007

Zhou Yue-Gang ,
Naoko Norioka ,
Li Shao-Liang  and
Shigemi Norioka
Zhou Yue-Gang*
Affiliation:
College of Bioengineering, Chongqing Institute of Technology, Chongqing 400050, China
Naoko Norioka
Affiliation:
Division of Protein Chemistry, Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan
Li Shao-Liang
Affiliation:
Division of Protein Chemistry, Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan
Shigemi Norioka
Affiliation:
Division of Protein Chemistry, Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan
*
*Corresponding author: Email: ygzhouc@yahoo.com.cn
Get access Rights & Permissions [Opens in a new window]

Abstract

A pollen cDNA library of Japanese pear (Pyrus pyrifolia) from the family Rosaceae was constructed and a cDNA (bgn-1) of 1408 bp, which encodes a protein (BGN-1) secreted from growing pollen tubes, was cloned and sequenced. bgn-1 cDNA is composed of a 5′-untranslated region of 47 bp, an open reading frame of 1194 bp encoding 397 amino acid residues and a complete 3′-untranslated region of 167 bp. Alignment of the deduced amino acid sequence of bgn-1 with that of barley (Hordeum vulgare) β-1,3-glucanase (GII) showed 39.7% amino acid identity. Several residues that were critical for the function of GII were conserved in the deduced BGN-1 polypeptide. Moreover, hydrophobic cluster analysis (HCA) showed an overall HCA homology score of 87.1% and analysis of BGN-1 with the 3D-PSSM program predicted a three-dimensional structure of BGN-1 highly homologous to that of barley GII with ≥95% certainty. These results suggest that the cloned bgn-1 cDNA encodes a β-1,3-glucanase-like protein in Japanese pear. The predicted mature protein (375 amino acids) has a theoretical molecular mass of 40 723 Da, a basic pI of 9.59 and a diagnostic amino acid residue mode of D, L, S and L, which is very similar to that of growth-related subfamily D (D, L, S and Q) in cereals. A ProXXPro repeat is also found between positions 352 and 367 in the C-extension region.

Keywords

cDNAβ-1,3-glucanasepollenPyrus pyrifolia
Type
Research Article
Information
Chinese Journal of Agricultural Biotechnology , Volume 2 , Issue 1 , April 2005 , pp. 53 - 58
Copyright
Copyright © China Agricultural University and Cambridge University Press 2005

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Callebaut, I, Labesse, G, Durand, P, Poupon, A, Canard, L, Chomilier, J et al. , (1997) Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cellular and Molecular Life Sciences 53: 621–645.Google Scholar
Cavener, DR and Ray, SC (1991) Eukaryotic start and stop translation sites. Nucleic Acids Research 19: 3185–3192.CrossRefGoogle ScholarPubMed
Futterer, J and Hold, T (1996) Translation in plants–rules and exceptions. Plant Molecular Biology 32: 159–189.CrossRefGoogle ScholarPubMed
Gaboriaud, C, Bissery, V, Benchetrit, T and Mornon, JP (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyze amino acid sequence. FEBS Letters 224: 149–155.Google Scholar
Ham, KS, Kauffmam, S, Albersheim, P and Darville, AG (1991) Host–pathogen interactions XXXIX. A soybean pathogenesis-related protein with β-1,3-glucanase activity releases phytoalexin elicitor-active heat-stable fragment from fungal walls. Molecular Plant–Microbe Interactions 4: 545–552.Google Scholar
Joshi, CP (1987) An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucleic Acids Research 15: 6643–6653.Google Scholar
Keen, NT and Yoshikawa, M (1983) β-1,3-Endoglucanase from soybean releases elicitor-active carbohydrates from fungus cell wall. Plant Physiology 71: 460–465.Google Scholar
Kelley, LA, MacCallum, RM and Sternberg, MJE (2000) Enhanced genome annotation using structural profiles in the program 3D-PSSM. Journal of Molecular Biology 299: 501–522.CrossRefGoogle ScholarPubMed
Kombrink, E and Somssich, IE (1995) Defense responses of plants to pathogens. Advances in Botanical Research 21: 1–34.CrossRefGoogle Scholar
Kozak, M (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44: 283–292.CrossRefGoogle ScholarPubMed
Mauch, F, Mauch-Mani, B and Boller, T (1988) Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and 1,3-β-glucanase. Plant Physiology 88: 936–942.Google Scholar
Romero, GO, Simmons, C, Yaneshita, M, Doan, M, Thomas, BR and Rodriguez, RL (1998) Characterization of rice endo-β-glucanase genes (Gns2–Gns14) defines a new subgroup within the gene family. Gene 223: 311–332.CrossRefGoogle ScholarPubMed
Rothnie, HM (1996) Plant mRNA 3′-end formation. Plant Molecular Biology 32: 43–61.CrossRefGoogle ScholarPubMed
Schlumbaum, A, Mauch, F, Vogeli, U and Boller, T (1986) Plant chitinases are potent inhibitors of fungal growth. Nature 324: 365–367.CrossRefGoogle Scholar
Stone, BA and Clarke, AE (1992) The Chemistry and Biology of (1→3)-β-Glucanase. Bundoora, Australia: La Trobe University Press.Google Scholar
Varghese, JN, Garrett, TPJ, Colman, PM, Chen, L, Hoj, PB and Fincher, GB (1994) Three-dimensional structures of two plant β-glucan endohydrolases with distinct substrate specificities. Proceedings of the National Academy of Sciences of the USA 91: 2785–2789.CrossRefGoogle ScholarPubMed
Xu, P, Wang, J and Fincher, GB (1992) Evolution and differential expression of the (1→3)-β-glucan endohydrolase-encoding gene family in barley, Hordeum vulgare. Gene 120: 157–165.Google Scholar