Autogenous regulation of the synthesis of ribosomal proteins, L10 and L7/12, in Escherichia coli
✍ Scribed by Fukuda, Ryuji
- Publisher
- Springer
- Year
- 1980
- Tongue
- English
- Weight
- 377 KB
- Volume
- 178
- Category
- Article
- ISSN
- 0026-8925
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A method is described by which ribosomal proteins L7L12 may be immunologically quantitated in the range of lo-75 pmol of protein. With this procedure the amount of ribosomal protein may be conveniently determined on the ribosome or in the postribosomal supernatant.
Knud Nierhaus, Who Has Studied The Ribosome For More Than 30 Years, Has Assembled Here The Combined Efforts Of Several Scientific Disciplines Into A Uniform Picture Of The Largest Enzyme Complex Found In Living Cells, Finally Resolving Many Decades-old Questions In Molecular Biology. In So Doing He
The structures of two prokaryotic ribosomal proteins, the carboxyterminal half of L7/L12 from Escherichia coli (L12CTF) and L30 from Bacilus stearothermophilus display a remarkably similar fold in which alpha-helices pack onto one side of an antiparallel, three-stranded, beta-pleated sheet. A detail
## Abstract Here we report the synthesis of the __N__‐terminal hexapeptide H‐Pro‐Arg‐Arg‐Arg‐Val‐Ile‐OH of the __E. coli__ ribosomal protein S7, the __C__‐terminal hexapeptide H‐Lys‐Glu‐Ala‐Lys‐Lys‐Lys‐OH of L6 and the __C__‐terminal hexapeptide H‐Pro‐Gln‐Val‐Leu‐Asp‐Ile‐OH of L13. All peptides wer