Lamin dimers. Presence in the nuclear lamin of surf clam oocytes and release during nuclear envelope breakdown

George N. Dessev, Christina Iovcheva-Dessev, Robert D. Goldman

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

The nuclear lamin of surf clam oocytes contains dimers of 67-kDa lamin which are stabilized by both noncovalent interactions and disulfide bonds. The latter can be reduced but re-form when the reducing agent is removed. The cysteine residues involved in these disulfide bonds are inaccessible to alkylating agents unless the protein is unfolded in urea. During nuclear envelope breakdown the lamin is released as a mixture of oligomers in which disulfide-stabilized dimers are associated noncovalently with lamin monomers. Concurrent with solubilization, both dimers and monomers are phosphorylated to a similar extent, indicating that the interactions which maintain these complexes are not destabilized by lamin phosphorylation. Our results suggest the existence of two types of interactions between the lamin molecules in the polymer, which react differently to phosphorylation during nuclear envelope breakdown.

Original languageEnglish (US)
Pages (from-to)12636-12641
Number of pages6
JournalJournal of Biological Chemistry
Volume265
Issue number21
StatePublished - 1990

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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