Ultraviolet inactivation of Escherichia coli ribosomes. II. Effects of messenger RNA binding on ultraviolet sensitivity of ribosomes

Tokimatsu, Hiroaki; Kagawa, Haruo; Fukutome, Hideo; Kawade, Yoshimi

doi:10.1016/0005-2787(68)90044-0

Cited by 11 publications

(3 citation statements)

References 5 publications

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“…Under conditions where 25% of the protein was crosslinked, the 30-S subunits lost 40% of their ability to reassociate with 50-S subunits and 80% of their activity in polyphenylalanine synthesis. This inactivation is in agreement with the study of Kagawa and coworkers [29,39,40], who observed that ultraviolet irradiation affects the association of the subunits, the binding of mRNA or tRNA and the synthesis of polyphenylalanine. The higher amount of inactivation (75%) than the yield of crosslinked protein (25%) could be explained by crosslinking of some other proteins to the 16-S RNA, but at a too-low yield to be characterised with our methodology.…”

Section: Discussionsupporting

confidence: 82%

Effect of Ultraviolet Irradiation on 30‐S Ribosomal Subunits. Identification of the RNA Region Crosslinked to Protein S7

Ehresmann

Backendorf

Ehresmann

et al. 1980

European Journal of Biochemistry

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The effects of ultraviolet irradiation on Escherichia coli 30-S ribosomal subunits were studied. At the doses of radiation used in this work (0-4.5 x lo5 quanta/30-S subunit), only protein S7 was found to be significantly crosslinked to the 16-S RNA. In conditions where 25 % of the protein was covalently crosslinked, the ability of the irradiated 30-S subunits to reassociate with 50-S subunits and their activity in polyphenylalanine synthesis decreased strongly. Similar results were obtained by irrradiation with a germicide lamp (254 nm) or with a monochromatic ultraviolet light at 248 nm. No additional proteins were crosslinked to the 16-S RNA by irradiating 30-S subunits depleted in protein S1 or 70-S ribosomes.The covalent complex of 16-S RNA and protein S7 was isolated and digested by TI ribonuclease.

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Section: Discussionsupporting

confidence: 82%

Effect of Ultraviolet Irradiation on 30‐S Ribosomal Subunits. Identification of the RNA Region Crosslinked to Protein S7

Ehresmann

Backendorf

Ehresmann

et al. 1980

European Journal of Biochemistry

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“…The two ribosomal subunits, whether or not they were associated, probably interacted with uv independently of each other; in addition, different partial functions of any one subunit may have been independently sensitive to radiation damage (Kagawa et al. 1967;Tokimatsu et al, 1968;Yasuda and Fukutome, 1970). Even the messengers, polyuridylic acid and TMV-RNA, probably had some heterogeneous character; for instance, their ability to bind to ribosomes and their ability to direct extended elongation of polypeptide chains may have been affected by uv differently.…”

Section: Discussionmentioning

confidence: 99%

Ultraviolet irradiation of the components of the wheat embryo in vitro protein synthesizing system

Murphy¹,

Kuhn²,

Murphy³

1973

Biochemistry

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“…the functional activity of the ribosomal subunits (Kagawa et al, 1967;Tokimatsu et al, 1968;Yasuda and Fukutome, 1970).…”

mentioning

confidence: 99%

Evidence for photoinduced crosslinkage, in situ, of 30S ribosomal proteins to 16S rRNA

Gorelic¹

1975

Biochemistry

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The effects of ultraviolet radiation on the 30S ribosomal subunit of Escherichia coli were studied. Irradiation in aqueous solution under anaerobic conditions resulted in a dose-dependent decrease in the separability of the rRNA and protein components of the 30S ribosomal subunit in 4 M urea-3 M LiC1. The results of gel filtration studies of the irradiated ribosomes before and after treatment with pancreatic ribonuclease indicated that the decrease in separability of the ribosome components was a result of the photoinduced formation of covalent RNA-protein cross-links. The number of covalent cross-links was estimated to correspond to less than 3 per 10,000 daltons of ribosomal proteins. One-dimensional gel electrophoresis studies of the course of the photoinduced cross-linkage reaction indicated that cross-linkage of individual 30S ribosomal proteins to the 16S rRNA proceeds in two dose-dependent steps. The first step requires an input of 1 X 10(20) quanta of 253.7 -nm radiation and results in the cross-linkage of at least five ribosomal proteins to the 16S rRNA. The second step requires a total input of 2 X 10(20) quanta of 253.7 -nm radiation, and results in the cross-linkage of most of the remaining 30S ribosomal proteins to the 16S rRNA.

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Ultraviolet inactivation of Escherichia coli ribosomes. II. Effects of messenger RNA binding on ultraviolet sensitivity of ribosomes

Cited by 11 publications

References 5 publications

Effect of Ultraviolet Irradiation on 30‐S Ribosomal Subunits. Identification of the RNA Region Crosslinked to Protein S7

Effect of Ultraviolet Irradiation on 30‐S Ribosomal Subunits. Identification of the RNA Region Crosslinked to Protein S7

Ultraviolet irradiation of the components of the wheat embryo in vitro protein synthesizing system

Evidence for photoinduced crosslinkage, in situ, of 30S ribosomal proteins to 16S rRNA

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