Decay of the oocyte-type heat shock response of Xenopus laevis

Leon W. Browder, M. Pollock, J. J. Heikkila, J. Wilkes, T. Wang, P. Krone, N. Ovsenek, Malgorzata Kloc

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

Xenopus oocytes have a complex heat shock response. During transition of the oocyte into fertilized egg, the heat shock response undergoes several qualitative and quantitative changes culminating in its complete extinction. Heat shock induces oocytes to synthesize four heat shock proteins (hsps): 83, 76, 70, and 57. After ovulation, two additional proteins (hsps 22 and 16) are inducible. The heat shock response of spawned eggs can be modified by changing the ionic configuration of the external medium and by adding pyruvate and oxaloacetate to the media. Since Xenopus eggs do not synthesize mRNA, these modifications to the external medium apparently alter the utilization of preexisting messenger RNAs in protein synthesis. Artificial activation terminates inducibility of hsps 76, 57, and 16 and diminishes the hsp 70 response. Two new heat shock proteins-66 and 48-are also inducible in artificially activated eggs. Fertilization, on the other hand, terminates the heat shock response; no hsps can be induced. However, hsp 70 appears to be made constitutively in fertilized eggs. RNA blot analyses reveal that oogenic hsp 70 messenger RNA is retained in eggs and early embryos. This messenger is apparently used for heat-induced synthesis of hsp 70 before fertilization and for constitutive synthesis of hsp 70 in zygotes.

Original languageEnglish (US)
Pages (from-to)191-199
Number of pages9
JournalDevelopmental Biology
Volume124
Issue number1
DOIs
StatePublished - Jan 1 1987

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

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