Identification of an endochitinase cDNA clone from barley aleurone cells

Swegle, Mark; Huang, Jenq‐Kuen; Lee, Grace; Muthukrishnan, Subbaratnam

doi:10.1007/bf00017580

Cited by 50 publications

(31 citation statements)

References 29 publications

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“…We provide evidence that the selectivity in the heat shock-induced suppression of normal cellular protein synthesis is drawn upon the distinction of secretary versus nonsecretory proteins. Northern blot analysis demonstrated heat have extended our studies to mRNAs encoding a secreted thiol endoprotease ( 11) and an endochitinase (19). By Northern blot analysis it was apparent that the levels of protease mRNA were markedly increased by the presence of GA3 (Fig.…”

Section: Discussionmentioning

confidence: 57%

“…Probes were made by nick-translating cloned cDNAs for the high-pI isozyme of a-amylase (pM/C) (14), the low-pI isozyme of a-amylase (clone E) (16), actin (pMAC-1) (17), endochitinase (19), protease (11), f3-tubulin (10), and three unidentified clones (nonGA3-inducible from barley aleurone layers) (L-S Lin, G Heck, T-hD Ho, unpublished data) in the presence of a-[32P]dCTP (New England Nuclear, specific activity >500 Ci/mmol).…”

Section: Rna Analysismentioning

confidence: 99%

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Heat Shock Causes Selective Destabilization of Secretory Protein mRNAs in Barley Aleurone Cells

Brodl

Ho²

1991

Plant Physiol.

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The aleurone layer of GA3-stimulated barley (Hordeum vulgare L., cv Himalaya) grains is normally devoted to the synthesis and secretion of hydrolytic enzymes. Heat shock, however, suppresses the synthesis of the main hydrolytic enzyme, a-amylase, by destabilizing its otherwise highly stable mRNA (FC Belanger, MR Brodl, T-hD Ho [1986] Proc Natd Acad Sci USA 83: 1354-1358. In this paper we document that heat shock causes the suppression of the synthesis of some normal cellular proteins, while the synthesis of other normal cellular proteins is unaffected by heat shock. There are two major isozymic forms of a-amylase encoded by distinct mRNAs. The mRNA levels for both isozymic forms and the mRNA levels of two other secretary proteins, a protease and an endochitinase, were markedly reduced during heat shock. However, the levels of actin and j-tubulin mRNAs, both nonsecretory proteins, were not diminished during heat shock. In addition, the levels of three other mRNA species detected by a set of unidentified cDNA clones (the sequence of one shows that it lacks a signal sequence) remained unchanged during heat shock. These data indicate that there are two classes of normal cellular protein mRNAs with regard to the effect of heat shock upon their persistence in the cell, and suggest that the distinction between them is whether or not they encode secretary proteins.Heat shock is, quite simply, a transient elevation in temperature, usually about 10 to 15oC above ambient temperature. This simple manipulation produces remarkable changes in gene expression. In every organism tested to date heat shock induces the synthesis of a characteristic set of proteins, the so-called hsps3 ( There is a translational bias established during heat shock that favors the translation of the newly transcribed hsp mRNAs (18). The mRNAs encoding normal cellular proteins persist in the cytoplasm; however, they are not translated during heat shock. When returned to normal temperatures, the synthesis of normal cellular proteins resumes even in the presence of actinomycin D, indicating that these mRNAs that had been quiescent during heat shock are reactivated during recovery (9).In yeast, the shift in gene expression is controlled at the transcriptional level. Heat shock induces the transcription of genes encoding hsps but represses the transcription of genes encoding normal cellular proteins. The normal cellular protein mRNAs already present in the cytoplasm continue to be translated (along with hsp mRNAs) until they are turned over at their normal, fairly rapid rates (13). In soybean a similar transcriptional regulation of normal cellular protein synthesis appears to be operating. Vierling and Key (20) have demonstrated that the mRNA for the small subunit of ribulose-1,5-phosphate carboxylase decreases during heat shock, presumably as it is turned over at its normal rate.We have previously investigated the heat-shock response in the cells of barley aleurone layers (2). a-Amylases are the principal enzymes synthesized and secreted by these ...

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Section: Discussionmentioning

confidence: 57%

Section: Rna Analysismentioning

confidence: 99%

Heat Shock Causes Selective Destabilization of Secretory Protein mRNAs in Barley Aleurone Cells

Brodl

Ho²

1991

Plant Physiol.

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“…Those CHs appear to be similar if not identical in tissue localization, amino acid sequence, and physical properties to CHs C and T, respectively (11,12 29) and cCHI26 (ref. 13), are derived from distinct genes, because the nucleotide sequences differ by 10% and their primary translation products differ in size.…”

Section: Discussionmentioning

confidence: 99%

“…During a previous study of genes expressed in the aleurone layer cells of germinating barley seeds, we identified a cDNA clone encoding a CH (29). Results of western blot analysis indicated the presence of at least two CHs in barley seeds.…”

mentioning

confidence: 99%

Properties of Barley Seed Chitinases and Release of Embryo-Associated Isoforms during Early Stages of Imbibition

Swegle¹,

Kramer²,

Muthukrishnan³

1992

Plant Physiol.

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Barley (Hordeum vulgare L.) seeds contain at least five proteins with chitinase (CH) activity. Two of these (CH1 and CH2) are found primarily in the aleurone and endosperm tissues, and the other three (CH3, CH4, and CH5) are enriched in the embryo. From the bran fraction, three of these CHs (CH1, CH2, and CH3) were purified to apparent homogeneity. These three CHs have apparent molecular masses of 27, 34, and 35 kilodaltons and isoelectric points of 9.3, 9.2, and 8.7, respectively. CH2 and CH3 have amino terminal sequences resembling a portion of the chitin-binding domain of lectins and other plant defense proteins. CH 1 lacks this domain. All three CHs exhibit antifungal activity and inhibit the mycelial growth of some species of Trichoderma and Fusarium in vitro. During the early period of imbibition by seeds, two of the embryo-associated CHs are selectively released into the surrounding aqueous medium. CHs2 (EC 3.2.1.14) catalyze the hydrolysis of 1(1,4) linkages between N-acetylglucosamine (2-acetamido-2-deoxyglucopyranoside) residues in the linear homopolymer, chitin.

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“…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).…”

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confidence: 99%

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

Kriz

Widholm

1994

Plant Physiol.

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Identification of an endochitinase cDNA clone from barley aleurone cells

Cited by 50 publications

References 29 publications

Heat Shock Causes Selective Destabilization of Secretory Protein mRNAs in Barley Aleurone Cells

Heat Shock Causes Selective Destabilization of Secretory Protein mRNAs in Barley Aleurone Cells

Properties of Barley Seed Chitinases and Release of Embryo-Associated Isoforms during Early Stages of Imbibition

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

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