Fragments of Ribosomal Protein S1 and Its Mutant Form m1‐S1: Localization of Nucleic‐Acid‐Binding Domain in the Middle Region of S1

Alap R. SUBRAMANIAN, Peter RIENHARDT, Makoto Kimura, Tangirala SURYANARAYANA

研究成果: ジャーナルへの寄稿記事

33 引用 (Scopus)

抄録

Escherichia coli ribosomal protein S1 and its mutant, shorter, form‐S1 were cleaved at internal methionyl residues to yield, respectively, six and five gragments of M ranging from 1000 to 24000. Methods are described to isolate the fragments in pure form. Four of the fragments (designated F2a, F2b, F3 and F4) contain between 86 and 215 amino acids and are therefore as large as other robosomal proteins. Fragments F2a, derived of S1 [S. Giorginis and A.R. Subramanian (1980) J. Mol. biol. 141, 393‐408]. Here we show that the RNA binding domain of S1 is essentially contained of S1, whose activity is modified by ligand binding, was localized in F2b, a fragment with little RNA binding capacity. The charaterisitic RNAbinding domain and a weak riosome binding domain of S1 have previously been localized in the large trypsin‐resistent core S1‐F1 [T. Suryanarayana and A.R. Subramanian (1979) J. Mol. Biol. 127, 41–54]. Together these date indicate that two of the key functional domains S1 are located in two regions of the molecule separated by an open, exposed segment. The present study also revealed that the nonreactive ‐SH group of S1 becomes reactive m1‐S1 by the loss of remote C‐terminal region in the latter.

元の言語英語
ページ(範囲)245-249
ページ数5
ジャーナルEuropean Journal of Biochemistry
119
発行部数2
DOI
出版物ステータス出版済み - 1 1 1981

Fingerprint

Escherichia coli Proteins
RNA
Ligands
Amino Acids
Escherichia coli
Proteins
Molecules
ribosomal protein S1
RNA-Binding Motifs

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

Fragments of Ribosomal Protein S1 and Its Mutant Form m1‐S1 : Localization of Nucleic‐Acid‐Binding Domain in the Middle Region of S1. / SUBRAMANIAN, Alap R.; RIENHARDT, Peter; Kimura, Makoto; SURYANARAYANA, Tangirala.

:: European Journal of Biochemistry, 巻 119, 番号 2, 01.01.1981, p. 245-249.

研究成果: ジャーナルへの寄稿記事

SUBRAMANIAN, Alap R. ; RIENHARDT, Peter ; Kimura, Makoto ; SURYANARAYANA, Tangirala. / Fragments of Ribosomal Protein S1 and Its Mutant Form m1‐S1 : Localization of Nucleic‐Acid‐Binding Domain in the Middle Region of S1. :: European Journal of Biochemistry. 1981 ; 巻 119, 番号 2. pp. 245-249.
@article{3115551a291e473188f94471d11b1428,
title = "Fragments of Ribosomal Protein S1 and Its Mutant Form m1‐S1: Localization of Nucleic‐Acid‐Binding Domain in the Middle Region of S1",
abstract = "Escherichia coli ribosomal protein S1 and its mutant, shorter, form‐S1 were cleaved at internal methionyl residues to yield, respectively, six and five gragments of M ranging from 1000 to 24000. Methods are described to isolate the fragments in pure form. Four of the fragments (designated F2a, F2b, F3 and F4) contain between 86 and 215 amino acids and are therefore as large as other robosomal proteins. Fragments F2a, derived of S1 [S. Giorginis and A.R. Subramanian (1980) J. Mol. biol. 141, 393‐408]. Here we show that the RNA binding domain of S1 is essentially contained of S1, whose activity is modified by ligand binding, was localized in F2b, a fragment with little RNA binding capacity. The charaterisitic RNAbinding domain and a weak riosome binding domain of S1 have previously been localized in the large trypsin‐resistent core S1‐F1 [T. Suryanarayana and A.R. Subramanian (1979) J. Mol. Biol. 127, 41–54]. Together these date indicate that two of the key functional domains S1 are located in two regions of the molecule separated by an open, exposed segment. The present study also revealed that the nonreactive ‐SH group of S1 becomes reactive m1‐S1 by the loss of remote C‐terminal region in the latter.",
author = "SUBRAMANIAN, {Alap R.} and Peter RIENHARDT and Makoto Kimura and Tangirala SURYANARAYANA",
year = "1981",
month = "1",
day = "1",
doi = "10.1111/j.1432-1033.1981.tb05600.x",
language = "English",
volume = "119",
pages = "245--249",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "2",

}

TY - JOUR

T1 - Fragments of Ribosomal Protein S1 and Its Mutant Form m1‐S1

T2 - Localization of Nucleic‐Acid‐Binding Domain in the Middle Region of S1

AU - SUBRAMANIAN, Alap R.

AU - RIENHARDT, Peter

AU - Kimura, Makoto

AU - SURYANARAYANA, Tangirala

PY - 1981/1/1

Y1 - 1981/1/1

N2 - Escherichia coli ribosomal protein S1 and its mutant, shorter, form‐S1 were cleaved at internal methionyl residues to yield, respectively, six and five gragments of M ranging from 1000 to 24000. Methods are described to isolate the fragments in pure form. Four of the fragments (designated F2a, F2b, F3 and F4) contain between 86 and 215 amino acids and are therefore as large as other robosomal proteins. Fragments F2a, derived of S1 [S. Giorginis and A.R. Subramanian (1980) J. Mol. biol. 141, 393‐408]. Here we show that the RNA binding domain of S1 is essentially contained of S1, whose activity is modified by ligand binding, was localized in F2b, a fragment with little RNA binding capacity. The charaterisitic RNAbinding domain and a weak riosome binding domain of S1 have previously been localized in the large trypsin‐resistent core S1‐F1 [T. Suryanarayana and A.R. Subramanian (1979) J. Mol. Biol. 127, 41–54]. Together these date indicate that two of the key functional domains S1 are located in two regions of the molecule separated by an open, exposed segment. The present study also revealed that the nonreactive ‐SH group of S1 becomes reactive m1‐S1 by the loss of remote C‐terminal region in the latter.

AB - Escherichia coli ribosomal protein S1 and its mutant, shorter, form‐S1 were cleaved at internal methionyl residues to yield, respectively, six and five gragments of M ranging from 1000 to 24000. Methods are described to isolate the fragments in pure form. Four of the fragments (designated F2a, F2b, F3 and F4) contain between 86 and 215 amino acids and are therefore as large as other robosomal proteins. Fragments F2a, derived of S1 [S. Giorginis and A.R. Subramanian (1980) J. Mol. biol. 141, 393‐408]. Here we show that the RNA binding domain of S1 is essentially contained of S1, whose activity is modified by ligand binding, was localized in F2b, a fragment with little RNA binding capacity. The charaterisitic RNAbinding domain and a weak riosome binding domain of S1 have previously been localized in the large trypsin‐resistent core S1‐F1 [T. Suryanarayana and A.R. Subramanian (1979) J. Mol. Biol. 127, 41–54]. Together these date indicate that two of the key functional domains S1 are located in two regions of the molecule separated by an open, exposed segment. The present study also revealed that the nonreactive ‐SH group of S1 becomes reactive m1‐S1 by the loss of remote C‐terminal region in the latter.

UR - http://www.scopus.com/inward/record.url?scp=0019629807&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019629807&partnerID=8YFLogxK

U2 - 10.1111/j.1432-1033.1981.tb05600.x

DO - 10.1111/j.1432-1033.1981.tb05600.x

M3 - Article

C2 - 7030733

AN - SCOPUS:0019629807

VL - 119

SP - 245

EP - 249

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 2

ER -