Nucleotide sequence of a rice genomic clone that encodes a class I endochitinase

A Review of the Applications of Chitin and Its Derivatives in Agriculture to Modify Plant-Microbial Interactions and Improve Crop Yields

“…From the early 1990s [136] onwards, a number of horticultural and agricultural crops have been genetically engineered to express foreign chitinases (summarized in Herrera-Estrella and Chet, 1999 [134]) in order to confer resistance to pathogens, pests and abiotic stress. As plant chitinases have been found to have a lower activity against insect pests, the chitinases used in transgenic crops are insect, bacterial or fungal in origin [137].…”

Molecular Analysis of Two cDNA Clones Encoding Acidic Class I Chitinase in Maize

“…The amino acid sequence of the barley protein (Leah et al, 1991) was compared with that of rice (Huang et al, 1991) to identify consensus sequences from which a pair of degenerate oligonucleotide primers were designed. Severa1 products were detected in the PCR, which ranged from about 300 to 700 bp on ethidium bromide-stained agarose gels (data not shown).…”

“…The asterisks indicate stop codons. Aligned amino acid sequences are presented for maize CHITA and CHITD (Hu),nh et al, 1992), rice RCC1 (Nishizawa and Hibi, 1991), rice class I (Huang et al, 1991), rice RCHlO (Zhu and Lamb,19Sll), barley CH126 (Leah et al, 1991), barley clonel0 (Swegle et al, 1989), bem CH18 (Broglie et al, 1986), bean PR4 (Mar1:isPinheiro et al, 1991), rapeseed CHB4 (Rasmussen et al, 1992), tobacco C H N 1 7 (Shinshi et al, 1990), and tobacco Tac.hl .…”

“…The primary structures and expression of various chitinases have been detennined in a variety of dicot and monocot plants (Swegle et al, 1989; Shinshi et al, 1990; Huang et al, 1991; Leah et al, 1991; Zhu and Lamb 1991; Huynh et al, 1992; Sela-Buurlage et al, 1993). These studies show that a11 stress-induced expression of chitinase activity is controlled by transcription rather than by enzyme activation, modification, or translation (Hedrick et al, 1988).…”

“…Class I chitinases are basic isoforms and may contain a Cysrich domain (also called the hevein domain), a hinge domain (Pro-, Gly-, and Arg-rich), and a major catalytic domain structure. Class I chitinases have been identified in tobacco (Shinshi et al, 1990), potato (Gaynor, 1988), bean (Broglie et al, 1986), Arabidopsis (Samac et al, 1990), and rice (Huang et al, 1991; Nishizawa and Hibi, 1991; Zhu and Lamb, 1991). Class I1 chitinases are acidic, lack the N-terminal Cys-rich domain and hinge domain, and have a high sequence similarity to class I chitinases within the catalytic domain.…”