Binding site of ribosomal proteins on prokaryotic 5S ribonucleic acids: a study with ribonucleases

S Douthwaite, A Christensen, R A Garrett

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 1982-May-11
OriginalsprogEngelsk
TidsskriftBiochemistry
Vol/bind21
Udgave nummer10
Sider (fra-til)2313-2320
Antal sider7
ISSN0006-2960
StatusUdgivet - 1982

Fingeraftryk

Ribosomal Proteins
Ribonucleases
Binding Sites
RNA
Escherichia coli Proteins
ribonuclease T(2)
Proteins
Ribonuclease T1
Pancreatic Ribonuclease
Biochemistry
Bacilli
Escherichia coli

Citer dette

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title = "Binding site of ribosomal proteins on prokaryotic 5S ribonucleic acids: a study with ribonucleases",
abstract = "The binding sites of ribosomal proteins L18 and L25 on 5S RNA from Escherichia coli were probed with ribonucleases A, T1, and T2 and a double helix specific cobra venom endonuclease. The results for the protein-RNA complexes, which were compared with those for the free RNA [Douthwaite, S., & Garrett, R. A. (1981) Biochemistry 20, 7301--7307], reveal an extensive interaction site for protein L18 and a more localized one for L25. Generally comparable results, with a few important differences, were obtained in a study of the binding sites of the two E. coli proteins on Bacillus stearothermophilus 5S RNA. Several protein-induced changes in the RNA structures were identified; some are possibly allosteric in nature. The two prokaryotic 5S RNAs were also incubated with total 50S subunit proteins from E. coli and B. stearothermophilus ribosomes. Homologous and heterologous reconstitution experiments were performed for both RNAs. The effects of the bound proteins on the ribonuclease digestion of the RNAs could generally be correlated with the results obtained with the E. coli proteins L18 and L25, although there was evidence for an additional protein-induced conformational change in the B. stearothermophilus 5S RNA, which may have been due to a third ribosomal protein L5.",
keywords = "Bacillus stearothermophilus, Bacterial Proteins, Binding Sites, Escherichia coli, Nucleic Acid Conformation, RNA, Bacterial, Ribonucleases, Ribosomal Proteins",
author = "S Douthwaite and A Christensen and Garrett, {R A}",
year = "1982",
language = "English",
volume = "21",
pages = "2313--2320",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "10",

}

Binding site of ribosomal proteins on prokaryotic 5S ribonucleic acids: a study with ribonucleases. / Douthwaite, S; Christensen, A; Garrett, R A.

I: Biochemistry, Bind 21, Nr. 10, 1982, s. 2313-2320.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Binding site of ribosomal proteins on prokaryotic 5S ribonucleic acids: a study with ribonucleases

AU - Douthwaite, S

AU - Christensen, A

AU - Garrett, R A

PY - 1982

Y1 - 1982

N2 - The binding sites of ribosomal proteins L18 and L25 on 5S RNA from Escherichia coli were probed with ribonucleases A, T1, and T2 and a double helix specific cobra venom endonuclease. The results for the protein-RNA complexes, which were compared with those for the free RNA [Douthwaite, S., & Garrett, R. A. (1981) Biochemistry 20, 7301--7307], reveal an extensive interaction site for protein L18 and a more localized one for L25. Generally comparable results, with a few important differences, were obtained in a study of the binding sites of the two E. coli proteins on Bacillus stearothermophilus 5S RNA. Several protein-induced changes in the RNA structures were identified; some are possibly allosteric in nature. The two prokaryotic 5S RNAs were also incubated with total 50S subunit proteins from E. coli and B. stearothermophilus ribosomes. Homologous and heterologous reconstitution experiments were performed for both RNAs. The effects of the bound proteins on the ribonuclease digestion of the RNAs could generally be correlated with the results obtained with the E. coli proteins L18 and L25, although there was evidence for an additional protein-induced conformational change in the B. stearothermophilus 5S RNA, which may have been due to a third ribosomal protein L5.

AB - The binding sites of ribosomal proteins L18 and L25 on 5S RNA from Escherichia coli were probed with ribonucleases A, T1, and T2 and a double helix specific cobra venom endonuclease. The results for the protein-RNA complexes, which were compared with those for the free RNA [Douthwaite, S., & Garrett, R. A. (1981) Biochemistry 20, 7301--7307], reveal an extensive interaction site for protein L18 and a more localized one for L25. Generally comparable results, with a few important differences, were obtained in a study of the binding sites of the two E. coli proteins on Bacillus stearothermophilus 5S RNA. Several protein-induced changes in the RNA structures were identified; some are possibly allosteric in nature. The two prokaryotic 5S RNAs were also incubated with total 50S subunit proteins from E. coli and B. stearothermophilus ribosomes. Homologous and heterologous reconstitution experiments were performed for both RNAs. The effects of the bound proteins on the ribonuclease digestion of the RNAs could generally be correlated with the results obtained with the E. coli proteins L18 and L25, although there was evidence for an additional protein-induced conformational change in the B. stearothermophilus 5S RNA, which may have been due to a third ribosomal protein L5.

KW - Bacillus stearothermophilus

KW - Bacterial Proteins

KW - Binding Sites

KW - Escherichia coli

KW - Nucleic Acid Conformation

KW - RNA, Bacterial

KW - Ribonucleases

KW - Ribosomal Proteins

M3 - Journal article

VL - 21

SP - 2313

EP - 2320

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 10

ER -