C23 interacts with B23, a putative nucleolar-localization-signal-binding protein.
Eur J Biochem
; 237(1): 153-8, 1996 Apr 01.
Article
in En
| MEDLINE
| ID: mdl-8620867
ABSTRACT
The human protein C23 (nucleolin) is a major nucleolar protein. Its interactions with other proteins were studied with the two-hybrid system which identified nucleolar protein B23 (nucleophosmin) as being associated with C23. Both proteins were co-immunoprecipitated from HeLa cell nuclear extract by either monoclonal anti-C23 or monoclonal anti-B23. Binding studies utilizing deletion mutants indicated that the binding of C23 and B23 involves specific motifs. In addition to an approximately 46-amino-acid-binding domain in B23 (amino acids 194-239), amino acids 540-628 of C23 were required for binding; this region of C23 is required for the nucleolar localization. In addition, nucleolar protein p120 was also found to be co-immunoprecipitated with B23. A fragment of p120 containing a functional nucleolar localization signal bound to the truncated binding domain of B23, as did C23. These results suggest that the interaction of C23 and B23 may represent a nucleolar-targeting mechanism in which B23 acts as a nucleolar-localization signal-binding protein.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Phosphoproteins
/
Protein Sorting Signals
/
Nuclear Proteins
/
RNA-Binding Proteins
/
Nucleolus Organizer Region
Limits:
Humans
Language:
En
Journal:
Eur J Biochem
Year:
1996
Document type:
Article