Abstract:
:The strong transactivation activity of the C-terminal half (amino acids 76-152) of Nm23 was reported previously. Here we examined a structural domain preventing or necessary to its transactivation activity. The C-terminal 1/4 (amino acids 109-152) was sufficient for transactivation, but the C-terminal half with a longer N-terminal extension (amino acids 58-152) caused the loss of the transactivation ability. Furthermore, coexpression of the N-terminal half with the C-terminus of Nm23-H1 blocked the transactivation activity of the C-terminal half, where direct interaction of both truncated proteins was demonstrated in vitro. Transactivation activities in the C-terminal halves of the known mutants (P96S, H118F, S120G, and S120A) exhibiting differential antimetastasis effects were also tested. Significant reduction of transactivation activity was observed only in H118F, indicating that NPD kinase active-site histidine is required. This suggests that transactivation potential of Nm23 is related to NDP kinase activity but not to metastasis suppressor activity.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Cho SJ,Lee NS,Jung YS,Lee H,Lee KJ,Kim E,Chae SKdoi
10.1006/bbrc.2001.6042subject
Has Abstractpub_date
2001-12-07 00:00:00pages
738-43issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(01)96042-5journal_volume
289pub_type
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journal_title:Biochemical and biophysical research communications
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