| 1. |
- Chang, Shu-Nu, 1975-, et al.
(författare)
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An acidic amino acid cluster regulates the nucleolar localization and ribosome assembly of human ribosomal protein L22
- 2000
-
Ingår i: FEBS Letters. - 0014-5793 .- 1873-3468. ; 484:1, s. 22-28
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Tidskriftsartikel (refereegranskat)abstract
- The control of human ribosomal protein L22 (rpL22) to enter into the nucleolus and its ability to be assembled into the ribosome is regulated by its sequence. The nuclear import of rpL22 depends on a classical nuclear localization signal of four lysines at positions 13-16. RpL22 normally enters the nucleolus via a compulsory sequence of KKYLKK (I-domain, positions 88-93). An acidic residue cluster at the C-terminal end (C-domain) plays a nuclear retention role. The retention is concealed by the N-domain (positions 1-9) which weakly interacts with the C-domain as demonstrated in the yeast two-hybrid system. Once it reaches the nucleolus, the question of whether rpL22 is assembled into the ribosome depends upon the presence of the N-domain. This suggests that the N-domain, on dissociation from its interaction with the C-domain, binds to a specific region of the 28S rRNA for ribosome assembly.
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| 2. |
- Chang, Shu-Nu, 1975-, et al.
(författare)
-
An acidic amino acid cluster regulates the nucleolar localization and ribosome assembly of human ribosomal protein L22
- 2000
-
Ingår i: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 484:1, s. 22-28
-
Tidskriftsartikel (refereegranskat)abstract
- The control of human ribosomal protein L22 (rpL22) to enter into the nucleolus and its ability to be assembled into the ribosome is regulated by its sequence. The nuclear import of rpL22 depends on a classical nuclear localization signal of four lysines at positions 13-16. RpL22 normally enters the nucleolus via a compulsory sequence of KKYLKK (I-domain, positions 88-93). An acidic residue cluster at the C-terminal end (C-domain) plays a nuclear retention role. The retention is concealed by the N-domain (positions 1-9) which weakly interacts with the C-domain as demonstrated in the yeast two-hybrid system. Once it reaches the nucleolus, the question of whether rpL22 is assembled into the ribosome depends upon the presence of the N-domain. This suggests that the N-domain, on dissociation from its interaction with the C-domain, binds to a specific region of the 28S rRNA for ribosome assembly.
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