Structure of Endochitinase Genes from Sugar Beets

Mikkelsen, Jørn Dalgaard; Berglund, Lars; Nielsen, Kristian; Christiansen, Henning; Bojsen, Kirsten

doi:10.1007/978-94-011-5942-5_40

Cited by 41 publications

(40 citation statements)

References 8 publications

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“…Immunoblotting of proteins was realized according to Wiweger et al (2003). Polyclonal antibodies against CH-4 ( Mikkelsen et al 1992) were used as primary antibodies. Alkaline phosphatase-labeled goat/antirabbit antibody (Sigma) diluted 1:30 000 in phosphate buffered saline pH 7.2 was used as a secondary antibody.…”

Section: Protein Extraction For Sds-page Of Agps Isoelectric Focusinmentioning

confidence: 99%

Protein expression during seed development in Araucaria angustifolia: transient accumulation of class IV chitinases and arabinogalactan proteins

Santos¹,

Wiethölter²,

Gueddari³

et al. 2006

Physiologia Plantarum

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Protein accumulation and patterns during embryogenesis in the recalcitrant seeds of the gymnosperm species Araucaria angustifolia (Bert.) O. Kuntze were studied. Soluble seed proteins, chitinases, and arabinogalactan proteins (AGPs) were analyzed by means of 2-D gel electrophoresis, mass spectrometry, isoelectric focusing, Western blot, precipitation and staining with b-glucosyl Yariv reagent (b-Glc) 3 Y, and gas liquid chromatography. Despite the recalcitrant nature of the seeds, the electrophoretic patterns of A. angustifolia seed proteins showed similarities with orthodox seed types. Proteins showing chitinolytic activity were observed in all seed stages analyzed, but the expression of class IV chitinases was restricted to late stages of seed development. AGPs were prominent during stages of seed development characterized by intensive cell division and differentiation, and their decrease during seed maturation might be related to cell wall modifications during the deposition of storage compounds. Gas liquid chromatographic analyzes of AGPs did not show quantitative changes in their carbohydrate moieties during seed development. A low molecular weight protein specifically expressed in mature seeds was precipitated using (b-Glc) 3 Y. Amino acid sequences obtained from MS/MS analysis revealed peptides rich in valine and acidic amino acids, but devoid in amino acids normally found in AGPs polypeptides, suggesting that these peptides are not related to classical or non-classical AGPs. Possible implications of chitinases and AGPs during seed development in A. angustifolia are discussed.

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Section: Protein Extraction For Sds-page Of Agps Isoelectric Focusinmentioning

confidence: 99%

Protein expression during seed development in Araucaria angustifolia: transient accumulation of class IV chitinases and arabinogalactan proteins

Santos¹,

Wiethölter²,

Gueddari³

et al. 2006

Physiologia Plantarum

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“…We propose a chitinase class IV to include the basic sugar beet chitinase IV (Mikkelsen et a/., 1992), the basic rape chitinase ChB4 (Rasmussen etal., 1992a(Rasmussen etal., ,1992b) as well as the acidic bean PR4 chitinase (Margis-Pinheiro et a/., 1991). These chitinases contain a cysteine-rich domain and a conserved main structure which resemble those of class I chitinases but are significantly smaller due to four deletions.…”

Section: Enzyme Activities Substrates and Biochemical Propertiesmentioning

confidence: 99%

“…The amino acid sequence identity of class IV chitinases with class I chitinases is only 4 1 4 7 % compared with 59433% identify between the individual chitinases of class IV and more than 69% identity between the individual chitinases of class I (Broglie et a/., 1986;Rasmussen etal., 1992a;Samac eta/., 1990;Shinshi etal., 1987Shinshi etal., , 1990. Furthermore, class IV and class I chitinases are serologically distinguishable (Mikkelsen et a/., 1992). A list of cloned chitinase genes is presented in Table 1.…”

Section: Enzyme Activities Substrates and Biochemical Propertiesmentioning

confidence: 99%

“…Class IV chitinases from sugar beet and rape, and some class I chitinases (designated Ib in Figure 1) from pea, rice and barley (Huang eta/., 1991;Mikkelsen et a/., 1992;Rasmussen et a/., 1992a;Swegle eta/., 1989;Vad, 1991) are synthesized without a C-terminal extension suggesting extracellular localization. The class IV chitinase fom sugar beet is indeed deposited in the apoplast (Mikkelsen et a/., 1992).…”

Section: Regulation Of Chitinasesmentioning

confidence: 99%

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Plant chitinases

Collinge¹,

Kragh²,

Mikkelsen³

et al. 1993

The Plant Journal

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792

528

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“…Through the breakdown of these components, the two hydrolases are thought to inhibit fungal growth. Four classes (I-IV) of plant endochitinases have been described (Mikkelsen et al, 1992), of which at least three are present in tobacco (Melchers et al, 1993a, and refs. therein).…”

Section: Chitinases and /3-13-glucanasesmentioning

confidence: 99%