抄録
The complete amino acid sequences of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui were determined. The sequences were established by manual sequencing of peptides produced with several proteases as well as by cleavage with dilute HCl. Proteins L16, L23 and L33 consist of 119, 154 and 69 amino acid residues, and their molecular masses are 13538, 16812 and 7620 Da, respectively. The comparison of their sequences with those of ribosomal proteins from other organisms revealed that L23 and L33 are related to eubacterial ribosomal proteins from Escherichia coli and Bacillus stearothermophilus, while protein L16 was found to be homologous to a eukaryotic ribosomal protein from yeast. These results provide information about the special phylogenetic position of archaebacteria.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 21-28 |
| ページ数 | 8 |
| ジャーナル | FEBS Letters |
| 巻 | 240 |
| 発行部数 | 1-2 |
| DOI | |
| 出版物ステータス | 出版済み - 11 21 1988 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
これを引用
The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui. / Hatakeyama, Tomomitsu; Hatakeyama, Tamiko; Kimura, Makoto.
：: FEBS Letters, 巻 240, 番号 1-2, 21.11.1988, p. 21-28.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui
AU - Hatakeyama, Tomomitsu
AU - Hatakeyama, Tamiko
AU - Kimura, Makoto
PY - 1988/11/21
Y1 - 1988/11/21
N2 - The complete amino acid sequences of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui were determined. The sequences were established by manual sequencing of peptides produced with several proteases as well as by cleavage with dilute HCl. Proteins L16, L23 and L33 consist of 119, 154 and 69 amino acid residues, and their molecular masses are 13538, 16812 and 7620 Da, respectively. The comparison of their sequences with those of ribosomal proteins from other organisms revealed that L23 and L33 are related to eubacterial ribosomal proteins from Escherichia coli and Bacillus stearothermophilus, while protein L16 was found to be homologous to a eukaryotic ribosomal protein from yeast. These results provide information about the special phylogenetic position of archaebacteria.
AB - The complete amino acid sequences of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui were determined. The sequences were established by manual sequencing of peptides produced with several proteases as well as by cleavage with dilute HCl. Proteins L16, L23 and L33 consist of 119, 154 and 69 amino acid residues, and their molecular masses are 13538, 16812 and 7620 Da, respectively. The comparison of their sequences with those of ribosomal proteins from other organisms revealed that L23 and L33 are related to eubacterial ribosomal proteins from Escherichia coli and Bacillus stearothermophilus, while protein L16 was found to be homologous to a eukaryotic ribosomal protein from yeast. These results provide information about the special phylogenetic position of archaebacteria.
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UR - http://www.scopus.com/inward/citedby.url?scp=0024294051&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(88)80333-8
DO - 10.1016/0014-5793(88)80333-8
M3 - Article
C2 - 3191994
AN - SCOPUS:0024294051
VL - 240
SP - 21
EP - 28
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-2
ER -