Polymerization of highly purified Tetrahymena 14-nm filament protein/citrate synthase into filaments and its possible role in regulation of enzymatic activity

Tetsuya Takeda, Yasuhiro Kurasawa, Yoshio Watanabe, Osamu Numata

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Tetrahymena 14-nm filament protein (49K protein) is a bifunctional protein with roles in the cytoskeleton and as citrate synthase. Previous studies in our laboratory showed that elongation factor 1α (EF-1α) copurifies with the 49K protein upon polymerization and depolymerization of the 49K protein. In this study, the 49K protein was isolated from partially purified 49K protein fraction containing EF-1α. Using the purified 49K protein and/or purified EF-1α, the interaction between 49K protein and EF-1α in filament formation was investigated electronmicroscopically and it was demonstrated that purified 49K protein was capable of forming 14-nm filaments without EF-1α. The 49K protein/citrate synthase has been suggested to form filaments in mitochondria. Here we show that the citrate synthase activity of 49K protein is decreased by polymerization and increased by depolymerization, suggesting a possible modulating mechanism of citrate synthase activity by monomer-polymer conversion in mitochondria in situ

Original languageEnglish
Pages (from-to)869-874
Number of pages6
JournalJournal of Biochemistry
Volume117
Issue number4
Publication statusPublished - Apr 1995
Externally publishedYes

Fingerprint

Tetrahymena
Citrate (si)-Synthase
Polymerization
Filament
Proteins
Protein
Peptide Elongation Factor 1
Elongation
Depolymerization
Mitochondria
Cytoskeleton
Polymers

Keywords

  • 14-nm filament
  • 14-nm filament protein/citrate synthase
  • Citrate synthase activity
  • EF-1α
  • Tetrahymena

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Molecular Biology
  • Biochemistry

Cite this

Polymerization of highly purified Tetrahymena 14-nm filament protein/citrate synthase into filaments and its possible role in regulation of enzymatic activity. / Takeda, Tetsuya; Kurasawa, Yasuhiro; Watanabe, Yoshio; Numata, Osamu.

In: Journal of Biochemistry, Vol. 117, No. 4, 04.1995, p. 869-874.

Research output: Contribution to journalArticle

@article{482e7e2a7c794b0e858939fd08a9add3,
title = "Polymerization of highly purified Tetrahymena 14-nm filament protein/citrate synthase into filaments and its possible role in regulation of enzymatic activity",
abstract = "Tetrahymena 14-nm filament protein (49K protein) is a bifunctional protein with roles in the cytoskeleton and as citrate synthase. Previous studies in our laboratory showed that elongation factor 1α (EF-1α) copurifies with the 49K protein upon polymerization and depolymerization of the 49K protein. In this study, the 49K protein was isolated from partially purified 49K protein fraction containing EF-1α. Using the purified 49K protein and/or purified EF-1α, the interaction between 49K protein and EF-1α in filament formation was investigated electronmicroscopically and it was demonstrated that purified 49K protein was capable of forming 14-nm filaments without EF-1α. The 49K protein/citrate synthase has been suggested to form filaments in mitochondria. Here we show that the citrate synthase activity of 49K protein is decreased by polymerization and increased by depolymerization, suggesting a possible modulating mechanism of citrate synthase activity by monomer-polymer conversion in mitochondria in situ",
keywords = "14-nm filament, 14-nm filament protein/citrate synthase, Citrate synthase activity, EF-1α, Tetrahymena",
author = "Tetsuya Takeda and Yasuhiro Kurasawa and Yoshio Watanabe and Osamu Numata",
year = "1995",
month = "4",
language = "English",
volume = "117",
pages = "869--874",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "4",

}

TY - JOUR

T1 - Polymerization of highly purified Tetrahymena 14-nm filament protein/citrate synthase into filaments and its possible role in regulation of enzymatic activity

AU - Takeda, Tetsuya

AU - Kurasawa, Yasuhiro

AU - Watanabe, Yoshio

AU - Numata, Osamu

PY - 1995/4

Y1 - 1995/4

N2 - Tetrahymena 14-nm filament protein (49K protein) is a bifunctional protein with roles in the cytoskeleton and as citrate synthase. Previous studies in our laboratory showed that elongation factor 1α (EF-1α) copurifies with the 49K protein upon polymerization and depolymerization of the 49K protein. In this study, the 49K protein was isolated from partially purified 49K protein fraction containing EF-1α. Using the purified 49K protein and/or purified EF-1α, the interaction between 49K protein and EF-1α in filament formation was investigated electronmicroscopically and it was demonstrated that purified 49K protein was capable of forming 14-nm filaments without EF-1α. The 49K protein/citrate synthase has been suggested to form filaments in mitochondria. Here we show that the citrate synthase activity of 49K protein is decreased by polymerization and increased by depolymerization, suggesting a possible modulating mechanism of citrate synthase activity by monomer-polymer conversion in mitochondria in situ

AB - Tetrahymena 14-nm filament protein (49K protein) is a bifunctional protein with roles in the cytoskeleton and as citrate synthase. Previous studies in our laboratory showed that elongation factor 1α (EF-1α) copurifies with the 49K protein upon polymerization and depolymerization of the 49K protein. In this study, the 49K protein was isolated from partially purified 49K protein fraction containing EF-1α. Using the purified 49K protein and/or purified EF-1α, the interaction between 49K protein and EF-1α in filament formation was investigated electronmicroscopically and it was demonstrated that purified 49K protein was capable of forming 14-nm filaments without EF-1α. The 49K protein/citrate synthase has been suggested to form filaments in mitochondria. Here we show that the citrate synthase activity of 49K protein is decreased by polymerization and increased by depolymerization, suggesting a possible modulating mechanism of citrate synthase activity by monomer-polymer conversion in mitochondria in situ

KW - 14-nm filament

KW - 14-nm filament protein/citrate synthase

KW - Citrate synthase activity

KW - EF-1α

KW - Tetrahymena

UR - http://www.scopus.com/inward/record.url?scp=0028954057&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028954057&partnerID=8YFLogxK

M3 - Article

C2 - 7592552

AN - SCOPUS:0028954057

VL - 117

SP - 869

EP - 874

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 4

ER -