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  Construction of the minimal SRP that interacts with the translating ribosome but not with specific membrane receptors in Escherichia coli

Avdeeva, O. N., Myasnikov, A. G., Sergiev, P. V., Bogdanov, A. A., Brimacombe, R., & Dontsova, O. A. (2002). Construction of the minimal SRP that interacts with the translating ribosome but not with specific membrane receptors in Escherichia coli. FEBS Letters, 514(1), 70-73.

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 Creators:
Avdeeva, Olga N., Author
Myasnikov, Alexander G., Author
Sergiev, Petr V., Author
Bogdanov, Alexey A., Author
Brimacombe, Richard1, Author           
Dontsova, Olga A., Author
Affiliations:
1Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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Free keywords: Signal recognition particle; Ribosome; Translation arrest; Ffh; 4.5S RNA
 Abstract: Escherichia coli signal recognition particle (SRP) consists of 4.5S RNA and Ffh protein. In contrast to eukaryotes, it remains unclear whether translation arrest takes place in prokaryotic cells. To study this problem we constructed a fusion of the M domain of Ffh protein with a cleavable affinity tag. This mutant Ffh, in a complex with 4.5S RNA, can bind signal peptide at the translating ribosome but is unable to bind the membrane. This SRP–ribosome complex should accumulate in the cell if translation is arrested. To test this, the complex was purified from the cells by ultracentrifugation and affinity chromatography. The composition of the complex was analyzed and found to consist of ribosomal RNAs and proteins, the Ffh M domain and 4.5S RNA. The accumulation of this complex in the cell in significant amounts indicated that SRP-mediated translation arrest did occur in bacterial cells.

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Language(s): eng - English
 Dates: 2002-03-06
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 24732
 Degree: -

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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 514 (1) Sequence Number: - Start / End Page: 70 - 73 Identifier: -