The role of expansion segment of human ribosomal protein L35 in nuclear entry, translation activity, and endoplasmic reticulum docking.
The phylogenic alignment of homologous L35 protein suggests that human large subunit ribosomal protein L35 carries a 54 aa eukaryotic expansion segment (ES) at the C-terminal end. Within this ES, the first 25 amino acid residues were found to be essential for the nuclear import of the protein. The last 29 residues of the ES were shown to be uninvolved in the ribosome's structural and translational functions, although this region proved to be one of the contact sites for ribosomal docking to endoplasmic reticulum, as evident from the results of an in vivo recombinant ribosome analysis.
Institute of Genetics, National Yang-Ming University, Shih-Pai, Taipei 112, Taiwan, ROC.
In-Jay
IJ
Chen
I-Ann
IA
Wang
Lin-Ru
LR
Tai
Alan
A
Lin
D021581:Active Transport, Cell Nucleus; D000595:Amino Acid Sequence; D002467:Cell Nucleus / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D019913:Nuclear Localization Signals; D014176:Protein Biosynthesis; D011994:Recombinant Proteins / Q000032:analysis; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D019913:Nuclear Localization Signals; C489281:RPL35A protein, human; D011994:Recombinant Proteins; D012269:Ribosomal Proteins