Mr 25 000 protein, a substrate for protein serine/threonine kinases, is identified as a part of Xenopus laevis vitellogenin B1

Satoshi Yoshitome, Hiroyasu Nakamura, Nobushige Nakajo, Kengo Okamoto, Isamu Sugimoto, Hiromi Kohara, Kaori Kitayama, Kazuaki Igarashi, Susumu Ito, Noriyuki Sagata, Eikichi Hashimoto

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Abstract

A phosphorylated protein with a molecular mass of 25 000 (pp25) previously purified from the cytosolic fraction of Xenopus laevis oocytes is an effective phosphate acceptor for casein kinases and protein kinase C. In this study, based on the partial amino acid sequence of pp25, a cDNA was isolated that encodes a new yolk precursor protein, Xenopus vitellogenin B1, which contained the sequence encoding pp25. Both mRNA and protein of vitellogenin B1 were expressed in all of the female organs examined. In agreement with a previous report, the amount of vitellogenin B1 protein in the liver increased after stimulation with estrogen. These results suggest that pp25 is a cytosolic non-crystallized yolk protein nutnent source, but it might also play a role in rapid development.

Original languageEnglish
Pages (from-to)283-294
Number of pages12
JournalDevelopment Growth and Differentiation
Volume45
Issue number3
DOIs
Publication statusPublished - Jun 2003

All Science Journal Classification (ASJC) codes

  • Developmental Biology
  • Cell Biology

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    Yoshitome, S., Nakamura, H., Nakajo, N., Okamoto, K., Sugimoto, I., Kohara, H., Kitayama, K., Igarashi, K., Ito, S., Sagata, N., & Hashimoto, E. (2003). Mr 25 000 protein, a substrate for protein serine/threonine kinases, is identified as a part of Xenopus laevis vitellogenin B1. Development Growth and Differentiation, 45(3), 283-294. https://doi.org/10.1046/j.1524-4725.2003.696.x