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Exchangeability of Qsr1p, a large ribosomal subunit protein required for subunit joining, suggests a novel translational regulatory mechanism
Author(s) -
Dick Frederick A,
Eisinger Dominic P,
Trumpower Bernard L
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01402-6
Subject(s) - eukaryotic large ribosomal subunit , ribosomal protein , eukaryotic small ribosomal subunit , protein subunit , ribosomal rna , eukaryotic ribosome , 5s ribosomal rna , specificity factor , cytoplasm , biology , chemistry , microbiology and biotechnology , ribosome , 18s ribosomal rna , biochemistry , rna , gene , rna dependent rna polymerase
Qsr1p is a 60S ribosomal subunit protein that is necessary for joining of large and small ribosomal subunits and is also one of the last proteins assembled onto the 60S ribosomal subunit in the cytoplasm. The finding that Qsr1p is identical to L7, a protein previously shown to cycle on and off large ribosomal subunits in the cytoplasm, suggests that the addition of Qsr1p onto the 60S ribosomal subunit could be utilized as a translational regulatory mechanism by limiting the supply of functional 60S subunits.