Primary structure of Escherichia coli ribosomal protein S1 and of its gene rpsA.

Schnier, Joachim; Kimura, Makoto; Foulaki, Kirani; Subramanian, Alap R.; Isono, Katsumi; Wittmann‐Liebold, Brigitte

doi:10.1073/pnas.79.4.1008

Cited by 59 publications

(17 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Simultaneously with the amino acid sequence determination of protein S1, the nucleotide sequence of the S1 gene (~p,rA) from E. coli 56.5 (a K12 strain) has been determined [37]. With the exception of two places, the deduced amino acid sequence of E. coli J6.5 protein S1 is in perrect agreement with the amino sequence given in Fig.7.…”

Section: Srruin-specific D I F F I~r C R~~s In Ilze Prirnury Srruciursupporting

confidence: 58%

See 1 more Smart Citation

Primary Structure of Escherichia coli Ribosomal Protein S1 and Features of Its Functional Domains

Kimura

Foulaki

Subramanian

et al. 1982

European Journal of Biochemistry

View full text Add to dashboard Cite

The complete covalent structure of ribosomal protein S1 of Eschericlziu coli has been determined and predictions made of its secondary structure. Protein S1 ( E . coli MRE 600) is a single-chain, acidic protein with 557 amino acid residues of the composition Asp43, Asn23, ThrZg, G I u~~, Glnl4, Prolo, Gly48, Ala48, Vab7, Metb, Ile30, Leu45, Tyr6, P1ieI7, Hiss, L Y S~~, Arg30, Trp7, C y s~ and an M , of 61 159. The two -SH groups of S1 are located in the central region of the chain at positions 292 and 349, the latter being the reactive group whose modification results in the reported loss of the nucleic-acid-unfolding ability of S1, The central region also contains the majority of the tryptophan, histidine and methionine residues of S1 and is predicted to have a secondary structure dominated by P-sheets and turns. A direct proof for the location of the nucleic-acid-binding domain of S1 in the central region has recently been obtained [Subramanian et al. (1981) Eur. J . Biochem. 119, 245-2491, The N-terminal region of S1, which contains the ribosome-binding domain has a relatively high predicted r-helix content and no preponderance of basic amino acids. The facile trypsin-sensitive site in S1 is located at Arg-171, approximately at the border between the N-terminal and central regions. The acidic and basic amino acids of S1 (32.8% of all residues) are distributed throughout the chain, often in small clusters of between two and six residues.The amino acid sequence of S1 contains three 24-residue stretches with strong internal homology. Two of the stretches are located in the central, RNA-binding region, suggesting a possible role in the RNA-binding and helix-destabilizing functions of S1. A fragment of M , lo4 from the central region of S1 gives an anomalously high apparent M , by dodecylsulfate gel electrophoresis, indicating a stable structural element therein and accounting for the apparent high M , of S1 as determined by gel electrophoresis.Protein S1 of Escherichia coli ribosome is the largest protein component of this organelle [I] and the largest of the four subunits of the phage-induced enzyme QP replicase [2] (see Discussion however). It is therefore a protein with potential u priori roles in the processes of both translation and transcription. Requirements of S1 for protein synthesis in vivo [3-81, i.e. for the binding of mRNA to ribosomes at the initiation step, and for Qfl RNA 'plus strand' replication have been established (reviewed in [9]). A mutant shorter form of S1 (mlS1) which is functionally active has been isolated [lo] and, with the aid of this mutation, the locus of the single S1 gene on the E. coli K12 chromosome has been mapped [I 11.Immune electron microscopy studies have localized S1 on the shoulder or on the platform-like structure on 30-S ribosomal subunits [12,13]. Chemical cross-linking experiments have crosslinked S1 to protein S2, S10 and S18 in 3 0 4 subunits and to initiation factors IF-2 and IF-3 in 70-S initiation complexes [14,15]. The distances between the reactive SH ...

show abstract

Section: Srruin-specific D I F F I~r C R~~s In Ilze Prirnury Srruciursupporting

confidence: 58%

“…In this paper we give a full description of the determination of the primary structure of S1 and report computer-assisted predictions of its secondary structure and features of its functional domains apparent from the data. A ,hart communication based on this work (and on tlie nucleotide Jequence of tlie S1 gene) has recently been published [37].…”

mentioning

confidence: 99%

Primary Structure of Escherichia coli Ribosomal Protein S1 and Features of Its Functional Domains

Kimura

Foulaki

Subramanian

et al. 1982

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…It has been reported that r-proteins S1 of several species have repeating amino acid residues in the central core and carboxyl terminal regions as mRNA-binding sites [13][14][15][16]. Also, it is well known that the mRNA binding to r-protein S1 in prokaryotes is the translation initiation reaction [3].…”

Section: Discussionmentioning

confidence: 99%

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

View full text Add to dashboard Cite

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.

show abstract

“…Here we describe the structure of one of these proteins, 1b11, in which the C-terminal region incorporates 34 residues from the E. coli 30S ribosomal protein S1 (Fig. 1B) (19). Both CspA ( Fig.…”

mentioning

confidence: 99%

A segment of cold shock protein directs the folding of a combinatorial protein

Bono

Riechmann²,

Girard³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

It has been suggested that protein domains evolved by the nonhomologous recombination of building blocks of subdomain size. In earlier work we attempted to recapitulate domain evolution in vitro. We took a polypeptide segment comprising three ␤-strands in the monomeric, five-stranded ␤-barrel cold shock protein (CspA) of Escherichia coli as a building block. This segment corresponds to a complete exon in homologous eukaryotic proteins and includes residues that nucleate folding in CspA. We recombined this segment at random with fragments of natural proteins and succeeded in generating a range of folded chimaeric proteins. We now present the crystal structure of one such combinatorial protein, 1b11, a 103-residue polypeptide that includes segments from CspA and the S1 domain of the 30S ribosomal subunit of E. coli. The structure reveals a segment-swapped, six-stranded ␤-barrel of unique architecture that assembles to a tetramer. Surprisingly, the CspA segment retains its structural identity in 1b11, recapitulating its original fold and deforming the structure of the S1 segment as necessary to complete a barrel. Our work provides structural evidence that (i ) random shuffling of nonhomologous polypeptide segments can lead to folded proteins and unique architectures, (ii ) many structural features of the segments are retained, and (iii ) some segments can act as templates around which the rest of the protein folds. molecular evolution ͉ unique architecture ͉ oligonucleotide͞ oligosaccharide-binding fold

show abstract

Primary structure of Escherichia coli ribosomal protein S1 and of its gene rpsA.

Cited by 59 publications

References 28 publications

Primary Structure of Escherichia coli Ribosomal Protein S1 and Features of Its Functional Domains

Primary Structure of Escherichia coli Ribosomal Protein S1 and Features of Its Functional Domains

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

A segment of cold shock protein directs the folding of a combinatorial protein

Contact Info

Product

Resources

About