Differential subcellular localization of ribosomal protein L7 paralogs in <Emphasis Type="Italic">Saccharomyces cerevisiae</Emphasis> |
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Authors: | Tae-Youl Kim Cheol Woong Ha Won-Ki Huh |
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Institution: | (1) School of Biological Sciences, and Research Center for Functional Cellulomics, Institute of Microbiology, Seoul National University, Seoul, 151-747, Korea |
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Abstract: | In Saccharomyces cerevisiae, ribosomal protein L7, one of the ∼46 ribosomal proteins of the 60S subunit, is encoded by paralogous RPL7A and RPL7B genes. The amino acid sequence identity between Rpl7a and Rpl7b is 97 percent; they differ by only 5 amino acid residues.
Interestingly, despite the high sequence homology, Rpl7b is detected in both the cytoplasm and the nucleolus, whereas Rpl7a
is detected exclusively in the cytoplasm. A site-directed mutagenesis experiment revealed that the change in the amino acid
sequence of Rpl7b does not influence its sub-cellular localization. In addition, introns of RPL7A and RPL7B did not affect the subcellular localization of Rpl7a and Rpl7b. Remarkably, Rpl7b was detected exclusively in the cytoplasm
in rpl7a knockout mutant, and overexpression of Rpl7a resulted in its accumulation in the nucleolus, indicating that the subcellular
localization of Rpl7a and Rpl7b is influenced by the intracellular level of Rpl7a. Rpl7b showed a wide range of localization
patterns, from exclusively cytoplasmic to exclusively nucleolar, in knock-out mutants for some rRNA-processing factors, nuclear
pore proteins, and large ribosomal subunit assembly factors. Rpl7a, however, was detected exclusively in the cytoplasm in
these mutants. Taken together, these results suggest that although Rpl7a and Rpl7b are paralogous and functionally replaceable
with each other, their precise physiological roles may not be identical. |
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Keywords: | GFP ribosomal protein L7 Saccharomyces cerevisiae subcellular localization |
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