The amino acid sequence of a small DNA binding protein from the archaebacterium Sulfolobus solfataricus

Makoto Kimura, Junko Kimura, Philippa Davie, Richard Reinhardt, Jan Dijk

研究成果: ジャーナルへの寄稿記事

43 引用 (Scopus)

抄録

The thermoacidophilic archaebacterium Sulfolobus solfataricus possesses several DNA binding proteins which may have a histone-like function. Two particularly dominant species have molecular masses of 7 and 10 kDa, respectively. We have purified one of the small proteins which occurs in a relatively large amount and have determined its amino acid sequence. The protein is characterized by a high lysine content; in the N-terminal region the lysine residues occur in an alternating order: X-K-X-K-X-K-X-K. The amino acid sequence does not indicate any obvious homology to those DNA binding proteins whose sequences have been determined.

元の言語英語
ページ(範囲)176-178
ページ数3
ジャーナルFEBS Letters
176
発行部数1
DOI
出版物ステータス出版済み - 10 15 1984

Fingerprint

Sulfolobus solfataricus
Archaea
DNA-Binding Proteins
Lysine
Amino Acid Sequence
Amino Acids
Molecular mass
Histones
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

これを引用

The amino acid sequence of a small DNA binding protein from the archaebacterium Sulfolobus solfataricus. / Kimura, Makoto; Kimura, Junko; Davie, Philippa; Reinhardt, Richard; Dijk, Jan.

:: FEBS Letters, 巻 176, 番号 1, 15.10.1984, p. 176-178.

研究成果: ジャーナルへの寄稿記事

Kimura, Makoto ; Kimura, Junko ; Davie, Philippa ; Reinhardt, Richard ; Dijk, Jan. / The amino acid sequence of a small DNA binding protein from the archaebacterium Sulfolobus solfataricus. :: FEBS Letters. 1984 ; 巻 176, 番号 1. pp. 176-178.
@article{6a27e059b5144e5f9e2548dfc3736f81,
title = "The amino acid sequence of a small DNA binding protein from the archaebacterium Sulfolobus solfataricus",
abstract = "The thermoacidophilic archaebacterium Sulfolobus solfataricus possesses several DNA binding proteins which may have a histone-like function. Two particularly dominant species have molecular masses of 7 and 10 kDa, respectively. We have purified one of the small proteins which occurs in a relatively large amount and have determined its amino acid sequence. The protein is characterized by a high lysine content; in the N-terminal region the lysine residues occur in an alternating order: X-K-X-K-X-K-X-K. The amino acid sequence does not indicate any obvious homology to those DNA binding proteins whose sequences have been determined.",
author = "Makoto Kimura and Junko Kimura and Philippa Davie and Richard Reinhardt and Jan Dijk",
year = "1984",
month = "10",
day = "15",
doi = "10.1016/0014-5793(84)80935-7",
language = "English",
volume = "176",
pages = "176--178",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - The amino acid sequence of a small DNA binding protein from the archaebacterium Sulfolobus solfataricus

AU - Kimura, Makoto

AU - Kimura, Junko

AU - Davie, Philippa

AU - Reinhardt, Richard

AU - Dijk, Jan

PY - 1984/10/15

Y1 - 1984/10/15

N2 - The thermoacidophilic archaebacterium Sulfolobus solfataricus possesses several DNA binding proteins which may have a histone-like function. Two particularly dominant species have molecular masses of 7 and 10 kDa, respectively. We have purified one of the small proteins which occurs in a relatively large amount and have determined its amino acid sequence. The protein is characterized by a high lysine content; in the N-terminal region the lysine residues occur in an alternating order: X-K-X-K-X-K-X-K. The amino acid sequence does not indicate any obvious homology to those DNA binding proteins whose sequences have been determined.

AB - The thermoacidophilic archaebacterium Sulfolobus solfataricus possesses several DNA binding proteins which may have a histone-like function. Two particularly dominant species have molecular masses of 7 and 10 kDa, respectively. We have purified one of the small proteins which occurs in a relatively large amount and have determined its amino acid sequence. The protein is characterized by a high lysine content; in the N-terminal region the lysine residues occur in an alternating order: X-K-X-K-X-K-X-K. The amino acid sequence does not indicate any obvious homology to those DNA binding proteins whose sequences have been determined.

UR - http://www.scopus.com/inward/record.url?scp=0021764377&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021764377&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(84)80935-7

DO - 10.1016/0014-5793(84)80935-7

M3 - Article

C2 - 6436055

AN - SCOPUS:0021764377

VL - 176

SP - 176

EP - 178

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -