The importin-beta P446L dominant-negative mutant protein loses RanGTP binding ability and blocks the formation of intact nuclear envelope.
J Cell Sci
; 115(Pt 8): 1675-87, 2002 Apr 15.
Article
in En
| MEDLINE
| ID: mdl-11950886
ABSTRACT
Three of the four independently induced Ketel(D) dominantnegative female sterile mutations that identify the Drosophila importin-beta gene, originated from a C4114--> T transition and the concurrent replacement of Pro446 by Leu (P446L). CD spectroscopy of representative peptides with Pro or Leu in the crucial position revealed that upon the Pro-->Leu exchange the P446L mutant protein loses flexibility and attains most likely an open conformation. The P446L mutation abolishes RanGTP binding of the P446L mutant form of importin-beta protein and results in increased RanGDP binding ability. Notably, the P446L mutant importin-beta does not exert its dominant-negative effect on nuclear protein import and has no effect on mitotic spindle-related functions and chromosome segregation. However, it interferes with nuclear envelope formation during mitosis-to-interphase transition, revealing a novel function of importin-beta.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Ran GTP-Binding Protein
/
Beta Karyopherins
/
Drosophila Proteins
/
Drosophila melanogaster
/
Mutation
/
Nuclear Envelope
Limits:
Animals
/
Female
/
Humans
Language:
En
Journal:
J Cell Sci
Year:
2002
Document type:
Article
Affiliation country:
Hungary