The α1-tubulin gene of Arabidopsis thaliana: primary structure and preferential expression in flowers

Steven R. Ludwig, David G. Oppenheimer, Carolyn D. Silflow, D. Peter Snustad

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Abstract

The primary structure of the α1-tubulin gene of Arabidopsis thaliana was determined and the 5′ and 3′ ends of its transcript were identified by S1 nuclease mapping experiments. The information obtained was used to (i) predict the amino acid sequence of the α1-tubulin, (ii) deduce the positions of introns within the α1-tubulin gene, and (iii) construct 3′ noncoding gene-specific hybridization probes with which to study the pattern of α1-tubulin transcript accumulation in different tissues and at different stages of development. The predicted amino acid sequence of the α1-tubulin has 92% identity with the predicted product of the previously characterized A. thaliana α3-tubulin gene. The coding sequence of the α1-tubulin gene is interrupted by four introns located at positions identical to those of the four introns in the α3 gene. RNA blot hybridization studies carried out with an α1-tubulin gene-specific probe showed that the α1 gene transcript accumulates primarily in flowers, with little transcript present in RNA isolated from roots or leaves. In order to investigate the pattern of α-tubulin gene expression in developing flowers, RNA was isolated from flowers at five different stages of development: flower buds, unopened flowers with pollen, open flowers, flowers with elongating carpels, and green seed pods. RNA blot hybridizations performed with 3′ noncoding gene-specific probes showed that the α3 tubulin gene transcript is present in flowers at all stages of development, whereas the α1-tubulin gene transcript could only be detected in RNA from unopened flowers with pollen, open flowers, and flowers with elongating carpels.

Original languageEnglish (US)
Pages (from-to)311-321
Number of pages11
JournalPlant molecular biology
Volume10
Issue number4
DOIs
StatePublished - Jul 1 1988

Keywords

  • gene structure
  • introns
  • protein homologies
  • transcript accumulation
  • tubulin

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