Calmodulin-like activity associated with chromatin from pea buds

Hideaki Matsumoto, Motokazu Tanigawa, Yamaya Tomoyuki

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)

Abstract

NAD kinase and cyclic AMP phosphodiesterase were activated by a factor prepared from pea chromatin. About 62% of the original amount of the factor in the purified chromatin was recovered in the reassociated chromatin.The NAD kinase- and cyclic AMP phosphodiesterase-activating factor was released from the chromatin by heat treatment with ethylene glycol-bis(β-aminoethyl ether)- N,N,N',N'-tetraacetic acid (EGTA) then adsorbed on an affinity gel of phenothiazineagarose derivatives in the presence of excess Ca2+ over EGTA, after which it was eluted by a flush of EGTA. Activation of NAD kinase and cyclic AMP phosphodiesterase by this factor depended on the presence of Ca2+.The NAD kinase-activating factor and chromatin were coeluted when soluble chromatin was applied to a Bio-Gel A50 column. When chromatin was chromatographed on the same column after digestion by DNase I, the factor was eluted in association with the digested products of the chromatin. The activation properties of this factor indicate that a calmodulin-like activity exists in association with pea chromatin.The activation curves of cyclic AMP phosphodiesterase with the pea bud factor and with bovine brain calmodulin were compared. The amount of the factor in the chromatin fraction that corresponded to authentic calmodulin was calculated as 5.7 μg per mg DNA.

Original languageEnglish
Pages (from-to)593-602
Number of pages10
JournalPlant and Cell Physiology
Volume24
Issue number4
DOIs
Publication statusPublished - 1983 Jun
Externally publishedYes

Keywords

  • Calcium
  • Calmodulin-like activity
  • Chromatin (pea)
  • Cyclic AMP phosphodiesterase
  • NAD kinase
  • Pisum sativum

ASJC Scopus subject areas

  • Physiology
  • Plant Science
  • Cell Biology

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