Presence and role of the 5SrRNA-L5 protein complex (5SRNP) in the threonyl- and histidyl-tRNA synthetase complex in rat liver cytosol

Ogata, Kazuhiro; Kurahashi, Ayumi; Nishiyama, Chikage; Terao, Kazuo

doi:10.1016/0167-4781(94)90192-9

Cited by 4 publications

(1 citation statement)

References 16 publications

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“…In rat liver, a complex of 5 S rRNA and L5 ribosomal protein was found to be associated with a high-molecular-mass complex of aminoacyl-tRNA synthetases [88] and complexes of threonyland histidyl-tRNA synthetases [89]. The presence of 5 S RNP in the macromolecular aminoacyl-tRNA synthetase complex enhanced the activities of methionyl-and isoleucyl-tRNA synthetases [90].…”

Section: Other Proteinsmentioning

confidence: 97%

5 S rRNA: structure and interactions

Szymański

Barciszewska

Erdmann

et al. 2003

Biochemical Journal

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5 S rRNA is an integral component of the large ribosomal subunit in all known organisms. Despite many years of intensive study, the function of 5 S rRNA in the ribosome remains unknown. Advances in the analysis of ribosome structure that have revealed the crystal structures of large ribosomal subunits and of the complete ribosome from various organisms put the results of studies on 5 S rRNA in a new perspective. This paper summarizes recently published data on the structure and function of 5 S rRNA and its interactions in complexes with proteins, within and outside the ribosome.

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Section: Other Proteinsmentioning

confidence: 97%

5 S rRNA: structure and interactions

Szymański

Barciszewska

Erdmann

et al. 2003

Biochemical Journal

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Extraribosomal functions of ribosomal proteins

Wool

1996

Trends in Biochemical Sciences

460

213

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Interaction of the Ribosomal Protein, L5, with Protein Phosphatase Type 1

Hirano

Hartshorne

1995

Journal of Biological Chemistry

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The two-hybrid system was used to screen for binding proteins of type 1 protein phosphatase. Two plasmids were constructed, one containing the cDNA of the delta isoform of the type 1 catalytic subunit and the other containing a chicken gizzard cDNA library. Yeast (Y190) were transformed with the plasmids and screened for interacting species. 35 positive clones were categorized into 19 gene groups. Most of these were not identified. One clone, however, contained a sequence identical to the C-terminal portion of the chicken ribosomal protein L5 and corresponded to nucleotide residues 606-975. L5 was isolated from rat liver ribosomes as the L5.5 S RNA complex. This activated phosphatase activity of a myosin-bound phosphatase and the isolated type 1 catalytic subunit using phosphorylated myosin light chains and phosphorylase alpha as substrates. In addition, it was found that phosphatase sedimented with ribosomal subunits containing L5 but did not sediment with those deficient in L5. These data indicate that L5 binds to the catalytic subunit of the type 1 protein phosphatase and may act as a target molecule for phosphatase in ribosomal function or other cell mechanisms.

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Presence and role of the 5SrRNA-L5 protein complex (5SRNP) in the threonyl- and histidyl-tRNA synthetase complex in rat liver cytosol

Cited by 4 publications

References 16 publications

5 S rRNA: structure and interactions

5 S rRNA: structure and interactions

Extraribosomal functions of ribosomal proteins

Interaction of the Ribosomal Protein, L5, with Protein Phosphatase Type 1

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