Small‐angle X‐ray scattering study of the 5S RNA binding proteins L18 and L25 from <i>Escherichia coli</i> ribosomes

Österberg, Ragnar; Sjöberg, Bo

doi:10.1016/0014-5793(76)80624-2

Cited by 29 publications

(3 citation statements)

References 21 publications

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“…On the other hand, protein LI, though it may be slightly asymmetric, does not appear to be as elongated from our study as it has been suggested to be in situ. Similarly, our results for L25 differ from those of small-angle X-ray scattering studies (Osterberg et al, 1976) which were peformed on a protein L25 that was isolated under denaturing conditions. Such proteins have been found to contain less tertiary structure (Morrison et al, 1977), and this could account for the observed differences.…”

Section: Discussioncontrasting

confidence: 99%

“…From immune electron microscopy [reviewed in Stoffler & Wittmann (1977)] and from small-angle X-ray scattering (Osterberg et al, 1976), elongated shapes have been inferred…”

Section: Discussionmentioning

confidence: 99%

“…The three antibody binding sites for LI are remote from each other, indicating an elongated shape in situ [reviewed in Brimacombe et al (1978)]. From a small-angle X-ray scattering study an elongated shape for protein L25 has been inferred (Osterberg et al, 1976).…”

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confidence: 99%

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Shapes of proteins L1, L9, L25, and L30 from the 50S subunit of the Escherichia coli ribosome, determined by hydrodynamic studies

Giri¹,

Franz²,

Dijk³

1979

Biochemistry

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Proteins L1, L9, L25, and L30, purified by a nondenaturing method from the 50S ribosomal subunit of Escherichia coli A19, have been characterized. The four proteins were studied under conditions which resemble those used for reconstitution experiments. These proteins have S020,W values of 2.0 S, 1.8 S, 1.8 S, and 1.0 S and D20,W values of 8.4 X 10(-7), 9.0 X 10(-7), 14.0 X 10(-7), and 15.0 X 10(-7) cm2/S. Apparent specific volumes at 20 degrees C are 0.738, 0.733, 0.700, and 0.735 mL/g for the four proteins. The respective molecular weights determined by sedimentation equilibrium are 25 000, 17 300, 12 000, and 6500. The intrinsic viscosity values for the four proteins are 4.0, 5.5, 3.6, and 3.2 mL/g. From these hydrodynamic parameters L1 and L9 appear to have globular or at most only slightly elongated shapes, whereas L25 and L30 appear to be definitely globular.

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Section: Discussioncontrasting

confidence: 99%

“…From immune electron microscopy [reviewed in Stoffler & Wittmann (1977)] and from small-angle X-ray scattering (Osterberg et al, 1976), elongated shapes have been inferred…”

Section: Discussionmentioning

confidence: 99%

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Shapes of proteins L1, L9, L25, and L30 from the 50S subunit of the Escherichia coli ribosome, determined by hydrodynamic studies

Giri¹,

Franz²,

Dijk³

1979

Biochemistry

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Chemical cross-linking of protein to RNA within intact ribosomal subunits from Escherichia coli

et al. 1978

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Bifunctional reagents, namely bis-(2-chloroethyl)-amine ("nitrogen mustard") and activated esters of 3-(2-bromo-3-oxobutane-1-sulphonyl)-propionic acid ("bromo-ketone reagent") are used to cross-linked protein to RNA within intact ribosomal subunits. The cross-linked proteins are analysed on two different two-dimensional gel electrophoresis sytems, and the existence of a stable cross-linkage is demonstrated by isolating cross-linked protein-oligonucleotide complexes from subunits containing 32P-labelled RNA. Proteins S3, S4, S5, S9/S11 and S13 from the 30S subunit, and proteins L1 and L2 from the 50S subunit were cross-linked to RNA by the nitrogen mustard, together with a number of other so far unresolved proteins. Correspondingly S3, S4, S7, S9/S11 and L12 were cross-linked by the bromoketone reagent, although in lower yield. The reagents should prove useful topographical studies on ribosomal subunits, and arguments are presented favouring the use of non-cleavable and relatively non-specific RNA-protein cross-linking reagents for such studies.

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Molecular interactions between ribosomal proteins — An analysis of S7-S9, S7-S19, S9-S19 and S7-S9-S19 interactions

Prakash

1988

J Biosci

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Small‐angle X‐ray scattering study of the 5S RNA binding proteins L18 and L25 from Escherichia coli ribosomes

Cited by 29 publications

References 21 publications

Shapes of proteins L1, L9, L25, and L30 from the 50S subunit of the Escherichia coli ribosome, determined by hydrodynamic studies

Shapes of proteins L1, L9, L25, and L30 from the 50S subunit of the Escherichia coli ribosome, determined by hydrodynamic studies

Chemical cross-linking of protein to RNA within intact ribosomal subunits from Escherichia coli

Molecular interactions between ribosomal proteins — An analysis of S7-S9, S7-S19, S9-S19 and S7-S9-S19 interactions

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