, Volume 231, Issue 5, pp 1127–1135 | Cite as

Onset of grain filling is associated with a change in properties of linker histone variants in maize kernels

  • Rainer Kalamajka
  • Christine Finnie
  • Klaus D. GrasserEmail author
Original Article


In maize kernel development, the onset of grain-filling represents a major developmental switch that correlates with a massive reprogramming of gene expression. We have isolated chromosomal linker histones from developing maize kernels before (11 days after pollination, dap) and after (16 dap) initiation of storage synthesis. Six linker histone gene products were identified by MALDI-TOF mass spectrometry. A marked shift of around 4 pH units was observed for the linker histone spot pattern after 2D-gel electrophoresis when comparing the proteins of 11 and 16 dap kernels. The shift from acidic to more basic protein forms suggests a reduction in the level of post-translational modifications of linker histones during kernel development. Analysis of their DNA-binding affinity revealed that the different linker histone gene products bind double-stranded DNA with similar affinity. Interestingly, the linker histones isolated from 16 dap kernels consistently displayed a lower affinity for DNA than the proteins isolated from 11 dap kernels. These findings suggest that the affinity for DNA of the linker histones may be regulated by post-translational modification and that the reduction in DNA affinity could be involved in a more open chromatin during storage synthesis.


Chromatin DNA interaction H1 Linker histone 2D-gel electrophoresis 



Days after pollination


Matrix-assisted laser desorption/ionisation–time-of-flight mass spectrometry


Trichloroacetic acid



This work was supported by grants from the Danish Research Council to Klaus Grasser. Rainer Kalamajka was recipient of a fellowship from the German Academic Exchance Service (DAAD).


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Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  • Rainer Kalamajka
    • 1
  • Christine Finnie
    • 2
  • Klaus D. Grasser
    • 1
    • 3
    Email author
  1. 1.Department of Life SciencesAalborg UniversityAalborgDenmark
  2. 2.Enzyme and Protein Chemistry, Building 224, Department of Systems BiologyTechnical University of DenmarkKgs. LyngbyDenmark
  3. 3.Cell Biology and Plant BiochemistryRegensburg UniversityRegensburgGermany

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