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Isolation and characterization of high-mobility-group proteins from maize

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Abstract

Chromosomal nonhistone high-mobility-group (HMG) proteins were purified from nuclei of maize (Zea mays L. cv. A619) endosperm and leaf tissue. Tissuespecific differences were observed in their polypeptide patterns, in in-vitro phosphorylation experiments with a casein-kinase type II, and by Western blot analysis with antisera against different HMG proteins. Gelfiltration chromatography demonstrated that maize HMG proteins occur as monomers. By measuring the capacity of the HMG proteins to bind to the 5′ flanking region of a zein gene, the sensitivity of the proteins to different temperatures, salt concentrations and pH values was determined.

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Abbreviations

EMSA:

electrophoretic-mobility-shift assay

FPLC:

fast protein liquid chromatography

HMG:

high-mobility group

kDa:

kilodaltons

PVDF:

polyvinylidenedifluoride

SDS-PAGE:

sodium dodecyl sulfate-polyacrylamide gel electrophoresis

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Authors and Affiliations

  1. Institut für Biologie III, Schänzlestrasse 1, W-7800, Freiburg, Germany

    Klaus D. Grasser, Andreas Wurz & Günter Feix

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  1. Klaus D. Grasser
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  2. Andreas Wurz
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  3. Günter Feix
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Additional information

We would like to thank Mrs. E. Brutzer for excellent technical assistance. We are indebted to Mrs. M. Strecker and Dr. W. Bessler of the Institut für Immunbiologie, Freiburg, FRG, for the preparation of antisera and we gratefully acknowledge helpful discussions with Drs. T. Quayle, R. Grimm and U. Müller of this institute. This work was supported by grants from the Deutsche Forschungsgemeinschaft and the Fond der Chemischen Industrie.

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Grasser, K.D., Wurz, A. & Feix, G. Isolation and characterization of high-mobility-group proteins from maize. Planta 185, 350–355 (1991). https://doi.org/10.1007/BF00201055

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