deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA helicase, can suppress a mutation in rpsB, the gene encoding ribosomal protein S2
| Autor: | K E Rudd, W M Toone, J D Friesen |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Ribosomal Proteins
Transcription Genetic Molecular Sequence Data Biology Microbiology Ribosomal protein Sequence Homology Nucleic Acid HSPA2 Escherichia coli Amino Acid Sequence Cloning Molecular Molecular Biology TAF15 Regulator gene Genetics Base Sequence Chromosome Mapping RNA Nucleotidyltransferases RNA Helicase A GPS2 EIF4EBP1 Genes Bacterial eIF4A Mutation RNA Helicases Research Article |
| Zdroj: | Journal of bacteriology. 173(11) |
| ISSN: | 0021-9193 |
| Popis: | We have cloned and sequenced a new gene from Escherichia coli which encodes a 64-kDa protein. The inferred amino acid sequence of the protein shows remarkable similarity to eIF4A, a murine translation initiation factor that has an ATP-dependent RNA helicase activity and is a founding member of the D-E-A-D family of proteins (characterized by a conserved Asp-Glu-Ala-Asp motif). Our new gene, called deaD, was cloned as a gene dosage-dependent suppressor of temperature-sensitive mutations in rpsB, the gene encoding ribosomal protein S2. We suggest that the DeaD protein plays a hitherto unknown role in translation in E. coli. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|