Structure qnd Functions of Ribosomal Protein S1

Subramanian, Alap R.

doi:10.1016/s0079-6603(08)60085-9

Cited by 265 publications

(309 citation statements)

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“…The r-protein S1 in Escherichia coli is well known to be associated with the 30S ribosomal subunit via its N-terminal globular domain. This protein has mRNA-binding sites and plays a key role in translation initiation by binding to mRNA in E. coli [3]. In this study, we report that anti-dsDNA antibodies immunoprecipitate 18S ribosomal RNA and suppress in vitro translation of mRNA.…”

Section: Introductionmentioning

confidence: 75%

“…It has been reported that the major function of r-protein S1 of E. coli in protein synthesis is at the mRNA binding step [3]. Thus this protein plays a key role in translation initiation in E. coli.…”

Section: Discussionmentioning

confidence: 99%

“…Also, it is well known that the mRNA binding to r-protein S1 in prokaryotes is the translation initiation reaction [3]. G7-RP as human r-protein S1 indeed contains these mRNA-binding sites [2].…”

Section: Discussionmentioning

confidence: 99%

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Autoantibodies to double-stranded (ds)DNA immunoprecipitate 18S ribosomal RNA by virtue of their interaction with ribosomal protein S1 and suppress in vitro protein synthesis

Tsuzaka

Winkler

Kalden

et al. 1996

Clinical and Experimental Immunology

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SUMMARYWe report that four systemic lupus erythematosus (SLE) patient sera containing anti-dsDNA antibodies, three affinity-purified anti-dsDNA IgG, and a human anti-dsDNA MoAb (33.H11) immunoprecipitate 18S ribosomal RNA from DNase-treated 32 P-labelled MOLT4 cell extract. This 18S RNA precipitation was inhibited completely by preincubating 33.H11 with calf thymus dsDNA or the recombinant human ribosomal protein S1, which was reported to cross-react with anti-dsDNA antibodies (J Immunol 1996; 156:1668-75). Whole IgG from three SLE sera with anti-dsDNA antibodies, 33.H11, and three affinitypurified anti-dsDNA IgG inhibited in vitro translation of globin mRNA (percent inhibition was 36-50%). This translation inhibition by anti-dsDNA antibodies was enhanced (67-79%) when the reticulocyte lysate was treated with DNase. Suppression of protein synthesis could be a pathogenic mechanism of anti-dsDNA antibodies, since it has also been shown that anti-dsDNA penetrates living cells (J Immunol 1995; 154:4857-64) in culture.

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Section: Introductionmentioning

confidence: 75%

Section: Discussionmentioning

confidence: 99%

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Autoantibodies to double-stranded (ds)DNA immunoprecipitate 18S ribosomal RNA by virtue of their interaction with ribosomal protein S1 and suppress in vitro protein synthesis

Tsuzaka

Winkler

Kalden

et al. 1996

Clinical and Experimental Immunology

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“…1. The interaction of initiation factor IF3 with the 3'-terminal loop of 16S RNA has also been analysed (Wickstrom, 1983); here it should be noted that an older report involving protein SI and this same RNA region now appears to represent a non-specific interaction (reviewed by Subramanian, 1983). In 23S RNA, protein LI has a well-defined and highly-conserved binding site (reviewed by Brimacombe et al, 1983), and the binding site of L23 has recently been described in detail (Vester & Garrett, 1984).…”

Section: Rna-protein Interactionmentioning

confidence: 99%

Structure and function of ribosomal RNA

Brimacombe¹,

Stiege²

1985

Biochemical Journal

107

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“…Ascribing to S1 a role at the initiation step is congenial with the traditional view of S1 as an RNA-binding protein whose function is attracting single-stranded RNA 15 . In the E. coli ribosome, S1 is thought to be involved in the initiation of protein synthesis by capturing mRNA 15 and/or unwinding the mRNA secondary structure 16,17 .…”

mentioning

confidence: 99%

Ribosomal protein S1 functions as a termination factor in RNA synthesis by Qβ phage replicase

et al. 2013

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S1 is the largest ribosomal protein, and is vitally important for the cell. S1 is also a subunit of Qb replicase, the RNA-directed RNA polymerase of bacteriophage Qb. In both protein and RNA syntheses, S1 is commonly believed to bind to a template RNA at the initiation step, and not to be involved in later events. Here, we show that in Qb replicase-mediated RNA synthesis, S1 functions at the termination step by promoting release of the product strand in a single-stranded form. This function is fulfilled by the N-terminal fragment comprising the first two S1 domains. The results suggest that S1 might also have a role other than mRNA binding in the ribosome.

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Structure qnd Functions of Ribosomal Protein S1

Cited by 265 publications

References 146 publications

Autoantibodies to double-stranded (ds)DNA immunoprecipitate 18S ribosomal RNA by virtue of their interaction with ribosomal protein S1 and suppress in vitro protein synthesis

Autoantibodies to double-stranded (ds)DNA immunoprecipitate 18S ribosomal RNA by virtue of their interaction with ribosomal protein S1 and suppress in vitro protein synthesis

Structure and function of ribosomal RNA

Ribosomal protein S1 functions as a termination factor in RNA synthesis by Qβ phage replicase

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