[39] Function of the ribosomal protein S1 in initiation and elongation of bacterial protein synthesis

Linde, R.; Manderschied, U.; Gassen, Hans Günter

doi:10.1016/s0076-6879(79)60041-1

Cited by 8 publications

(3 citation statements)

References 13 publications

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“…S1 interacts with the 30S subunit and 70S ribosomes (Draper and von Hippel, 1979), with E. coli RNA polymerase (Sukhodolets and Garges, 2003; Sukhodolets et al, 2006; Demo et al, 2017a), and is an integral part of the Q phage replisome (Takeshita et al, 2014). In translation, S1 may play multiple roles, including those in translation initiation (Khanh et al, 1979; Tedin et al, 1997; Sørensen et al, 1998; Delvillani et al, 2011; Duval et al, 2013), elongation (Khanh et al, 1979; Potapov and Subramanian, 1992; Sørensen et al, 1998), tmRNA-mediated ribosome rescue (McGinness and Sauer, 2004; Saguy et al, 2007) and possibly ribosome recycling (Delvillani et al, 2011). The best understood role for S1 is in translation initiation where S1 is required for translation of mRNAs with structured 5′ ends or with weak or no Shine-Dalgarno sequences (Duval et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM

Loveland

Коростелев

2018

Methods

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Bacterial ribosomal protein S1 is the largest and highly flexible protein of the 30S subunit, and one of a few core ribosomal proteins for which a complete structure is lacking. S1 is thought to participate in transcription and translation. Best understood is the role of S1 in facilitating translation of mRNAs with structured 5' UTRs. Here, we present cryo-EM analyses of the 70S ribosome that reveal multiple conformations of S1. Based on comparison of several 3D maximum likelihood classification approaches in Frealign, we propose a streamlined strategy for visualizing a highly dynamic component of a large macromolecular assembly that itself exhibits high compositional and conformational heterogeneity. The resulting maps show how S1 docks at the ribosomal protein S2 near the mRNA exit channel. The globular OB-fold domains sample a wide area around the mRNA exit channel and interact with mobile tails of proteins S6 and S18. S1 also interacts with the mRNA entrance channel, where an OB-fold domain can be localized near S3 and S5. Our analyses suggest that S1 cooperates with other ribosomal proteins to form a dynamic mesh near the mRNA exit and entrance channels to modulate the binding, folding and movement of mRNA.

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Section: Introductionmentioning

confidence: 99%

Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM

Loveland

Коростелев

2018

Methods

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“…The second conclusion is a consequence of the new Sl-free system described in this paper. In most of the previous Sl-free systems described in the literature (Tal et al, 1972;Van Dieijen et al, 1975;Khanh et al, 1979), the background activity in the absence of added SI is quite high. For this reason, the observed stimulation by SI has not been very striking.…”

Section: Discussionmentioning

confidence: 97%

An essential function of ribosomal protein S1 in mRNA translation

Suryanarayana¹,

Subramanian²

1983

Biochemistry

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A gentle and efficient method for selectively removing S1 from ribosomes was developed: the S1-free translation system prepared from such ribosomes is stimulated 10-20-fold (depending on the mRNA) by a stoichiometric amount of added purified S1. With this system, we examined the activity of mono- and di-N-ethylmaleimide derivatives of S1 in protein synthesis using synthetic and natural mRNAs and electrophoretic analysis of the translation products. The results show that ribosomes containing such modified S1's are functionally active although at a somewhat lower level (50-80% activity). Since treatment of S1 with N-ethylmaleimide abolishes the helix-destabilizing ability of S1, we conclude that this ability is not primarily responsible for S1's biological function. A new model for the role of S1 is proposed on the basis of the physical, structural, and RNA-binding properties of S1.

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“…Evidence was obtained which indicated that EF-3 was essential for the translation of natural mRNA as well as poly(U), was associated with polysomes but not ribosomal subunits, and was required for every cycle in the elongation phase of protein synthesis. factors, have been prepared (Howe et al, 1978;Petryshyn et al, 1979; Khanh et al, 1979;Van Duin et al, 1979;Lelong et al, 1979; Zinker, 1980;Politz & Glitz, 1980;Ghosh-Dastidar et al, 1980;Tanaka et al, 1980;Stoffler et al, 1980;Kahan et al, 1981;Fahnestock et al, 1981; Van Duin & Wijnands, 1981; Kastner et al, 1981;Brown-Luedi et al, 1982;Meyer et al, 1982;Howe & Hershey, 1982;Olson et al, 1982). One of the problems inherent in the use of polyclonal antibodies has been the requirement for pure specific proteins for immunization, which in many cases are available only in 0006-2960/84/0423-3055S01.50/0 © 1984 American Chemical Society limited quantities, require laborious purification procedures, and may exhibit a low degree of immunogenicity.…”

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confidence: 99%

Monoclonal antibody specific for yeast elongation factor 3

Hutchison¹,

Feinberg²,

Rothwell³

et al. 1984

Biochemistry

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Hybridomas have been prepared by fusing mouse myeloma (P3 X 63 Ag8) cells with spleen cells of mice immunized with a yeast fraction enriched with respect to non-ribosomal translational components. Cloned hybridoma lines were grown in the form of ascites tumors, and the monoclonal antibodies produced were purified from the ascites fluid by chromatography on DEAE-Affi-Gel Blue. One of the antibodies, from a hybridoma cell line designated as PSH-1, inhibited the translation of natural mRNA and poly(U) and polysomal chain elongation in a cell-free protein-synthesizing system from yeast. Resolution and partial purification of the elongation factors indicated that the monoclonal antibody from PSH-1 did not interact with EF-1 or EF-2 but reacted with and inactivated EF-3, the 125 000 molecular weight additional elongation factor specifically required with yeast ribosomes. The EF-3 purified from the cytosol by immunoaffinity chromatography was comparable to that prepared by ion-exchange chromatography. Evidence was obtained which indicated that EF-3 was essential for the translation of natural mRNA as well as poly(U), was associated with polysomes but not ribosomal subunits, and was required for every cycle in the elongation phase of protein synthesis.

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[39] Function of the ribosomal protein S1 in initiation and elongation of bacterial protein synthesis

Cited by 8 publications

References 13 publications

Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM

Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM

An essential function of ribosomal protein S1 in mRNA translation

Monoclonal antibody specific for yeast elongation factor 3

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