Compact globular structure of protein S15 from <i>Escherichia coli</i> ribosomes

Gogia, Z.V.; Venyaminov, Sergei Yu.; Bushuev, V.N.; Serdyuk, Igor N.; Lim, V.I.; Spirin, Alexander S.

doi:10.1016/0014-5793(79)80888-1

Cited by 18 publications

(9 citation statements)

References 28 publications

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“…We think that small values of radii of gyration will always mean a high degree of tertiary folding as has already been shown for proteins S15 [6], S4 [7], S7 (this communication and [S]), S8 [5,15] and S16 [5,15,16].…”

Section: Pimentioning

confidence: 59%

“…Protein S7 from the 30 S subunit of E. coli MRE-600 ribosomes was isolated and prepared as described for proteins S4 and S15 in our previous communications [6,7]. The identity, purity and homogeneity of protein S7 were checked by two-dimensional gel electrophoresis in urea, one-dimensional gel electrophoresis in sodium dodecyl sulfate, N-terminal group determination and amino acid analysis.…”

Section: Methodsmentioning

confidence: 99%

“…Circular dichroism (CD) spectra were measured with a J41A JASCO instrument as described earlier for proteins S4 and S1.5 [6,7]. For calculation of the ellipticity the mean molecular weight of the residue (MRW) was assumed to be 111.5 [2].…”

Section: Elsevierjnorth-holland Biomedical Pressmentioning

confidence: 99%

“…Proton NMR spectra were recorded on a Bruker WH-360 Fourierspectrometer as described earlier for proteins S4 and S1.5 [6,7]. Fig.1 presents the ultraviolet absorption spectrum of protein S7 recorded in the buffer containing 0.05 M sodium phosphate, pH 7 .O.…”

Section: Elsevierjnorth-holland Biomedical Pressmentioning

confidence: 99%

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Study of the secondary and tertiary structure of ribosomal protein S7 from Escherichia coli in solution

et al. 1981

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Section: Pimentioning

confidence: 59%

Section: Methodsmentioning

confidence: 99%

Section: Elsevierjnorth-holland Biomedical Pressmentioning

confidence: 99%

Section: Elsevierjnorth-holland Biomedical Pressmentioning

confidence: 99%

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Study of the secondary and tertiary structure of ribosomal protein S7 from Escherichia coli in solution

et al. 1981

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“…On the other hand, a number of ribosomal proteins, such as S4, S7, S8, S15, and S16, have been reinvestigated and found to be compact globular proteins with cooperative tertiary structures (23)(24)(25). Based on these new results and using the numerous data reported on mutual arrangement (topography) of ribosomal proteins, we have constructed a model of the quaternary structure of the ribosomal 30S particle and then checked it by neutron and x-ray scattering experiments.…”

mentioning

confidence: 99%

Quaternary structure of the ribosomal 30S subunit: model and its experimental testing.

Spirin¹,

Serdyuk²,

Shpungin³

et al. 1979

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

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In considering the structure of the 30S subunit of the Escherichia coli ribosome, we have assumed that: (l) all or almost all the proteins within the 30S particle are compact and globular, as recently shown for the isolated proteins S4, S7, S8, S15, and S16 in solution [Serdyuk, I. N., Zaccai, G. & Spirin, A. S. (1978) In recent years, the technique of chemical crosslinking of neighboring proteins by bifunctional reagents and measurements of the distances between deuterated or fluorescent-labeled proteins by using neutron scattering or energy transfer techniques, respectively, have contributed much to the knowledge of the protein topography in ribosomal particles and especially in the ribosomal 30S subunit of Escherichia coli. From these and a number of less direct data, several models of the topography of ribosomal proteins in the 30S particle have been proposed (1)(2)(3)(4)(5)(6)(7)(8). Independently, the use of the immunoelectron microscopy technique has also led to two different models of the topography of ribosomal proteins on the surface of the 30S particle (9-12; see also ref. 13).However, two complications have hampered further progress. First, no information was available as to three-dimensional structure and morphology of the 16S RNA; this RNA is known to be a structural backbone for arrangement of ribosomal proteins. Second, immunoelectron microscopy (9, 10) and neutron scattering (14, 15) data on proteins within the 30S subunit, as well as some physical measurements of isolated ribosomal proteins (16-21), have suggested strongly elongated or very expanded shapes of many ribosomal proteins; this led to ambiguity in interpretation of the results on chemical crosslinking, energy transfer, etc.Most recently, a specific compact conformation of the 16S RNA has been visualized by electron microscopy (22). On the other hand, a number of ribosomal proteins, such as S4, S7, S8, S15, and S16, have been reinvestigated and found to be compact globular proteins with cooperative tertiary structures (23)(24)(25). Based on these new results and using the numerous data reported on mutual arrangement (topography) of ribosomal proteins, we have constructed a model of the quaternary structure of the ribosomal 30S particle and then checked it by neutron and x-ray scattering experiments.MODEL CONSTRUCTION Initial Assumptions. In constructing the model, we have adhered to the size and the asymmetric three-dimensional structure of the ribosomal 30S subunit first deduced by one of us from electron microscopy of freeze-dried and shadow-cast samples of the particles (26). Morphologically, the 30S particle was found to be subdivided into a "head," a "body," and a side "bulge" (Fig. 1). A similar subdivision of the 30S particles, with a side "platform," was reported also by Lake and Kahan (11) and Lake (27) on the basis of electron microscopy of negatively stained samples.We have proceeded from two principal assumptions: (i) RNA within the 30S particle has a specific V-like or Y-like conformation (Fig. 1), as it is visu...

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Application of Ring Current Calculations to the Proton NMR of Proteins and Transfer RNA

Perkins

1982

Biological Magnetic Resonance

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Compact globular structure of protein S15 from Escherichia coli ribosomes

Cited by 18 publications

References 28 publications

Study of the secondary and tertiary structure of ribosomal protein S7 from Escherichia coli in solution

Study of the secondary and tertiary structure of ribosomal protein S7 from Escherichia coli in solution

Quaternary structure of the ribosomal 30S subunit: model and its experimental testing.

Application of Ring Current Calculations to the Proton NMR of Proteins and Transfer RNA

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