Binding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulin

N Kourmouli, G Dialynas, C Petraki, A Pyrpasopoulou, P B Singh, S D Georgatos, P A Theodoropoulos

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

We have previously shown that the mouse heterochromatin protein 1 homologue M31 interacts dynamically with the nuclear envelope. Using quantitative in vitro assays, we now demonstrate that this interaction is potently inhibited by soluble factors present in mitotic and interphase cytosol. As indicated by depletion and order-of-addition experiments, the inhibitory activity co-isolates with a 55-kDa protein, which binds avidly to the nuclear envelope and presumably blocks M31-binding sites. Purification of this protein and microsequencing of tryptic peptides identify it as alpha2/6:beta2-tubulin. Consistent with this observation, bona fide tubulin, isolated from rat brain and maintained in a nonpolymerized state, abolishes binding of M31 to the nuclear envelope and aborts M31-mediated nuclear envelope reassembly in an in vitro system. These observations provide a new example of "moonlighting," a process whereby multimeric proteins switch function when their aggregation state or localization is altered.

Original languageEnglish
Pages (from-to)13007-14
Number of pages8
JournalJournal of Biological Chemistry
Volume276
Issue number16
DOIs
Publication statusPublished - Apr 20 2001

Fingerprint

Nuclear Envelope
Tubulin
Carrier Proteins
Proteins
Purification
Rats
Assays
Brain
Interphase
Agglomeration
Binding Sites
Switches
Cytosol
Peptides
heterochromatin-specific nonhistone chromosomal protein HP-1
Experiments
In Vitro Techniques

Keywords

  • Amino Acid Sequence
  • Animals
  • Brain
  • Chromosomal Proteins, Non-Histone
  • Endometrial Neoplasms
  • Female
  • HeLa Cells
  • Heterochromatin
  • Humans
  • Kinetics
  • Mice
  • Molecular Sequence Data
  • Molecular Weight
  • Nuclear Envelope
  • Peptide Fragments
  • Protein Binding
  • Recombinant Proteins
  • Tubulin
  • Tumor Cells, Cultured
  • Journal Article
  • Research Support, Non-U.S. Gov't

Cite this

Kourmouli, N., Dialynas, G., Petraki, C., Pyrpasopoulou, A., Singh, P. B., Georgatos, S. D., & Theodoropoulos, P. A. (2001). Binding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulin. Journal of Biological Chemistry, 276(16), 13007-14. https://doi.org/10.1074/jbc.M007135200

Binding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulin. / Kourmouli, N; Dialynas, G; Petraki, C; Pyrpasopoulou, A; Singh, P B; Georgatos, S D; Theodoropoulos, P A.

In: Journal of Biological Chemistry, Vol. 276, No. 16, 20.04.2001, p. 13007-14.

Research output: Contribution to journalArticle

Kourmouli, N, Dialynas, G, Petraki, C, Pyrpasopoulou, A, Singh, PB, Georgatos, SD & Theodoropoulos, PA 2001, 'Binding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulin', Journal of Biological Chemistry, vol. 276, no. 16, pp. 13007-14. https://doi.org/10.1074/jbc.M007135200
Kourmouli, N ; Dialynas, G ; Petraki, C ; Pyrpasopoulou, A ; Singh, P B ; Georgatos, S D ; Theodoropoulos, P A. / Binding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulin. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 16. pp. 13007-14.
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