Complex formation between ribosomal protein S1, oligo-and polynucleotides: chain length dependence and base specificity

Lipecky, Rolf; Kohlschein, J′′rgen; Gassen, Hans G″nter

doi:10.1093/nar/4.10.3627

Cited by 39 publications

(17 citation statements)

References 26 publications

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“…One difference between our results and those of Lipecky et al (1977) deserves comment. We found weaker Si binding as the Mg2+ concentration was increased, whereas they found the contrary.…”

Section: Revision Of the Bulge Loop Entropy Parameterscontrasting

confidence: 80%

“…Our results do not require such a hypothesis, since the strong complex of Sl and colicin fragment has 1:1 stoichiometry. Similarly, the results of Lipecky et al (1977) imply a 1:1 complex for binding of Un, 7 < n < 14, to Si protein. Direct investigation of this question will require experiments capable of measuring independently the simultaneous Si binding of two distinct oligonucleotide species.…”

Section: Revision Of the Bulge Loop Entropy Parametersmentioning

confidence: 63%

“…On the other hand, physical (Bear et al, 1976;Szer et al, 1976;Draper et al, 1977;Lipecky et al, 1977) and other studies (Tal et al, 1972;Miller and Wahba, 1974;Miller et al, 1974;Carmichael, 1975;Jay and Kaempfer, 1975;Senear and Steitz, 1976;Goelz and Steitz, 1977) have shown that S1 protein exhibits strong affinity for pyrimidine-rich singlestranded regions in RNA. The association constant we measure for the Sl-colicin fragment interaction (5 x 106 M 1 at 40C, 5 mM Mg 2+, 100 mtM KCl) is comparable to the value obtained by Lipecky et al (1977) for the Sl-U12 complex (9 x 106 at 40C, 10 mM Mg2+, 200 mM NaCl). Thus we cannot rule out the possibility that the strong Sl-colicin fragment interaction is an accidental consequence of the presence in the RNA of a pyrimidine-rich region.…”

Section: Revision Of the Bulge Loop Entropy Parametersmentioning

confidence: 96%

“…Possibly this reflects increased stabilization of the bulge helix, whose melting is required for binding as the Mg2+ concentration is increased in our system. The oligo U molecules studied by Lipecky et al (1977) are expected to have little secondary structure, and hence Mg2+ should not interfere with binding because RNA melting is not required. The results reported by Szer et al (1976) on the binding of Si to MS2 RNA showed decreased affinity as Mg2+ was increased, probably because RNA melting is required, just as in our system.…”

Section: Revision Of the Bulge Loop Entropy Parametersmentioning

confidence: 99%

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The 3′ terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1

et al. 1979

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We report studies of the secondary structure and S1 ribosomal protein binding properties of the colicin fragment, containing 49 residues from the 3' terminus of E. coli 16S rRNA. Temperature jump relaxation kinetic measurements reveal two helices in the structure. One of these, melting at 81 degrees C in 5 mM Mg2+, is associated with the 9-base pair hairpin helix predicted by the nucleotide sequence. The other melting transition, at 21 degrees C in 5 mM Mg2+, is assigned to a 4-base pair helix which constrains the pyrimidine tract of the colicin fragment into a bulge loop. S1 protein forms a strong 1:1 complex with the colicin fragment, with an association constant of 5 x 10(6) M-1 in 5 mM Mg2+. More protein molecules are bound, but with weaker affinity, when the S1 concentration is increased. S1 binding causes melting of the colicin fragment secondary structure, as inferred from the observed absorbance increase. The S1 binding site on the colicin fragment has been localized in the region of the bulge loop, since the melting transition corresponding to the 4-base pair helix is lost in the complex. We discuss current models for the role of S1 protein in polypeptide chain initiation in light of these and previous results.

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“…One difference between our results and those of Lipecky et al (1977) deserves comment. We found weaker Si binding as the Mg2+ concentration was increased, whereas they found the contrary.…”

Section: Revision Of the Bulge Loop Entropy Parameterscontrasting

confidence: 80%

Section: Revision Of the Bulge Loop Entropy Parametersmentioning

confidence: 63%

Section: Revision Of the Bulge Loop Entropy Parametersmentioning

confidence: 96%

Section: Revision Of the Bulge Loop Entropy Parametersmentioning

confidence: 99%

See 2 more Smart Citations

The 3′ terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1

et al. 1979

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“…Protein S1 is a very elongated protein of about the same length as the ribosome (-250 A) according to various physical measurements (7)(8)(9)(10). It is a strong RNA binding protein and is capable of unwinding double-stranded regions in RNA structure (11)(12)(13)(14). According to recent studies (15)(16)(17), protein S1 is organized into two distinct functional domains-one for binding to the ribosome and the other for binding to RNA.…”

mentioning

confidence: 99%

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

Schnier¹,

Kimura²,

Foulaki³

et al. 1982

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

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The primary structure of protein SI, the largest protein component of the Escherichia coli ribosome, has been elucidated by determining the amino acid sequence of the protein (from E. coli MRE600) and the nucleotide sequence of the SI gene (rpsA, of a K-12 strain). The two methods gave results in perfect agreement except at two positions where possible strain-specific differences were found. Protein S1 (MRE600) is composed of 557 amino acid residues (no modified amino acids were detected) and has Mr 61,159. The DNA sequence for protein SI (K-12) suggests 556 amino acid residues. A computer survey of the sequence revealed three regions in S1 with a high degree ofinternal homology. The ribosome binding domain of SI (NH2 terminus) does not show any preponderance ofbasic amino acids. The two cysteine and the majority of tryptophan residues of S1 as well as two of the three homologous regions are located in its middle region which contains the nucleic acid binding domain. The pattern of degenerate codon usage in the S1 gene is nonrandom and similar to that reported for other ribosomal protein genes.Protein S1 ofthe Escherichia coli ribosome is the largest protein component of this organelle (1). There have been some questions earlier about its stoichiometry in ribosomes but it is now established that S1 is present in one copy per ribosomal particle (2,3). In addition to its occurrence in ribosomes, protein S1 is also a component of the multimeric enzyme Qf3 replicase (4) found in E. coli cells infected with bacteriophage Q,3.Studies from several laboratories (e.g., refs. 5 and 6) have established an essential role-for S1 in the initiation of protein synthesis by E. coli ribosomes, but the exact nature of this role has not been elucidated. Protein S1 is a very elongated protein of about the same length as the ribosome (-250 A) according to various physical measurements (7-10). It is a strong RNA binding protein and is capable of unwinding double-stranded regions in RNA structure (11)(12)(13)(14). According to recent studies (15-17), protein S1 is organized into two distinct functional domains-one for binding to the ribosome and the other for binding to RNA.The structural gene for S1 (rpsA) has been mapped at 20 min on the E. coli K-12 chromosome (18) and a transducing A phage carrying rpsA (ASerC) has been isolated (19). It therefore is feasible to determine the primary structure of protein S1 by both protein and DNA sequence determination procedures. The two methods, when combined, shorten the time required for establishing the primary structure of a protein of the size of S1. Knowledge of the primary structure of S1 would help to understand the various functions associated with this protein.In this paper we report the primary structure of S1 as determined by both protein and DNA sequences and some essential features of this structure.MATERIALS AND METHODS Protein Sequence. Protein S1 was isolated from E. coli MRE600. The protein was cleaved with CNBr to yield six fragments which were isolated in pure form (...

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Functional Characterization of Some Ribosomal Proteins from Wheat Germ

Legocki¹,

Madrzak²,

Przybyl³

et al. 1980

Genome Organization and Expression in Plants

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Complex formation between ribosomal protein S1, oligo-and polynucleotides: chain length dependence and base specificity

Cited by 39 publications

References 26 publications

The 3′ terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1

The 3′ terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1

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

Functional Characterization of Some Ribosomal Proteins from Wheat Germ

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