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Related Experiment Videos

Galactosylserine in extensin.

D T Lamport, L Katona, S Roerig

    The Biochemical Journal
    |May 1, 1973
    PubMed
    Summary

    Tomato cell walls contain extensin with O-glycosidically linked galactose residues on serine. This galactosylserine linkage is sensitive to alkali and hydrazine, indicating a specific glycosylation site on extensin.

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    Area of Science:

    • Plant Cell Wall Biology
    • Glycobiology
    • Protein Chemistry

    Background:

    • Tomato cell walls contain extensin, a hydroxyproline-rich glycoprotein.
    • Extensins are known to be post-translationally modified with carbohydrates.

    Purpose of the Study:

    • To investigate the glycosylation pattern of extensin in tomato cell walls.
    • To identify the specific amino acid residues and linkage types of galactose attachment.

    Main Methods:

    • Acid hydrolysis of tomato cell walls to remove arabinose substituents.
    • Tryptic digestion to isolate glycopeptides.
    • Alkaline hydrolysis (NaOH-NaBH4, NaOH-Na2SO3) and hydrazinolysis to analyze glycosidic linkages.
    • Chemical modification (maleylation, 3-carboxypropionylation) of N-terminal serine.

    Main Results:

    • Acid-stripped cell walls yielded glycopeptides containing galactose.
    • Alkaline treatment and hydrazinolysis of a specific glycopeptide (S2A6) resulted in the loss of galactose and conversion of serine to alanine or cysteic acid.
    • Chemical modification of N-terminal serine was required for complete galactose loss, indicating O-glycosidic linkage to serine residues.
    • Hydrazinolysis destroyed non-glycosylated serine but not glycosylated serine, confirming the galactosylserine linkage sensitivity.

    Conclusions:

    • A single galactose residue is attached O-glycosidically to two serine residues within the extensin glycopeptide S2A6.
    • The galactosylserine linkage is sensitive to alkaline conditions and hydrazinolysis.
    • This study elucidates a specific glycosylation site and linkage type in plant extensin.

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