FEBS Letters
Volume 580, Issue 16 , Pages 3804-3810, 10 July 2006

Mapping the essential structures of human ribosomal protein L7 for nuclear entry, ribosome assembly and function

Edited by Lev Kisselev

Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan, ROC

Received 26 January 2006; received in revised form 23 May 2006; accepted 23 May 2006. published online 14 June 2006.

Abstract 

Human large subunit protein L7 carries multiple nuclear localization signals (NLS) in its structure: there are three monobasic partite NLSs at the NH2-region of the first 54 amino acid residues and a bipartite in the middle section at position of 156–167. The C-region of the last 50 amino acid residues displays membrane binding nature, and might involve in forming a nuclear microbody for pre-nucleolar ribosome assembly. The middle section covers 144 amino acid residues which are essential for the structure and function of ribosome. This is evident from findings that truncated L7 without the NH2-region or the C-region, or missing both regions, is capable of reaching nucleolus and incorporating in ribosome, however, only ribosomes bearing truncated L7 without the NH2-region is capable of engaging in polysome formation. Combining with the phylogenic findings from homologous sequence alignment, the NH2-region of L7, besides being as a eukaryotic expansion segment, can be excluded from building a functional eukaryotic ribosome.

Keywords: Nuclear localization signal, Eukaryotic ribosomal protein, Ribosome assembly, Ribosome expansion segment, Nuclear microbody

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PII: S0014-5793(06)00691-0

doi:10.1016/j.febslet.2006.05.073

FEBS Letters
Volume 580, Issue 16 , Pages 3804-3810, 10 July 2006