Animal cells and systems

The Korean Society for Integrative Biology (한국통합생물학회)
권호 표지

The C-terminal Region of Human Tau Protein with Ability of Filament Formation

  • Chung, Sang-Ho (Department of MicroBiology, College of Science and Technology, Mokwon University)
  • Published : 1997.06.01
Download PDF
⟨ Previous Next ⟩

Abstract

Tau protein is one of the microtubule-associated proteins in the mammalian brain. In Alzheimer's disease, tau protein is immobilized in the somatodendritic compartment of certain nerve cells, where it forms a part of the paired helical filament (PHF). To understand the role of tau protein in the formation of PHF, a recombinant human tau protein expressed in Escherichia coli and five synthetic peptide fragments (peptide 1 to peptide 5), corresponding to the C-terminal region of tau protein, were prepared and their ability in self-assembly to form filamentous structures was examined. The recombinant human tau protein formed short rod-like structures in 0.1M MES buffer containing 1 mM $MgCI_2$, while a synthetic peptide fragment 1 containing 55 amino acid residues could assemble into a lot of long filamentous structures in water and particularly twisted helical structures in 0.1M MES buffer containing 1 mM $MgCI_2$. This suggests that the C-terminal region possesses a filament-forming ability and may be related to the formation of the helical structure by providing a powerful filament-forming driving force.

Keywords

References

  1. EMBO J v.11 The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region Biernat J;Mandelkow EM;Schroter C;Lichtenberg-Kraag B;Steiner B;Berling B;Meyer H;Mercken M;Vandermeeren A;Goedert M;Mandelkow E
  2. Biochem J v.273 Tau in Alzheimer neurofibrillary tangles, N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site Brion JP;Hanger DP;Bruce MT;Couck AM;Flament-Durand J;Anderson BH
  3. Korean J Microbiol v.32 Cloning and expression of a human tau gene cDNA in Escherichia coli Chung SH;Maeda T;Yanagawa H
  4. J Mol Biol v.116 Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin Cleveland DW;Hwo SY;Kirschner MW
  5. Eur J Biochem v.176 A new siliconized-glass fiber as support for protein-chemical analysis of electroblotted proteins Eckerskorn C;Mewes W;Goretzki H;Lottspeich F
  6. EMBO J v.9 Expression of separate isoforms of human tau protein: correlation with tau pattern in brain and effects on tubulin polymerization Goedert M;Jakes R
  7. Neuron v.3 Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease Goedert M;Spillantini MG;Jakes R;Rutherford D;Crowther RA
  8. EMBO J v.8 Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain Goedert M;Spillantini MG;Potier MC;Ulrich J;Crowther RA
  9. Proc Natl Acad Sci USA v.85 Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau Goedert M;Wischik CW;Crowther RA;Walker JE;Klug A
  10. J Biol Chem v.261 Microtubule-associated protein tau. A component of Alzheimer paired helical filaments Grundke-Iqbal I;Iqbal K;Quinlan M;Tung YC;Zaidi MS;Wisniewski HM
  11. Proc Natl Acad Sci USA v.83 Abnormal phosphorylation of the microtubule-associated protein τ (tau) in Alzheimer cytoskeletal pathology Grundke-Iqbal I;Iqbal K;Tung YC;Quinlan M;Wisniewski HM;Binder L
  12. J Cell Biol v.109 Tau protein becomes long and stiff upon phosphorylation: Correlation between paracrystalline structure and degree of phosphorylation Hagestedt T;Lichtenberg B;Wille H;Mandelkow EM;Mandelkow E
  13. Mol Cell Biol v.9 Structure of the bovine tau gene: Alternatively spliced transcripts generate a protein family Himmler A
  14. Mol Cell Biol v.9 Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains Himmler A;Drechsel D;Kirschner MW;Martin DW Jr
  15. J Cell Biol v.107 Tau protein: the molecular structure and mode of binding on microtubules Hirokawa N;Shiomura Y;Okabe S
  16. Annu Rev Biochem v.49 Blood coagulation Jackson CM;Nemerson Y
  17. EMBO J v.10 Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease Jakes R;Novak M;Davison M;Wischik CM
  18. J Cell Biol v.109 Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA Kanai Y;Takemura R;Oshima T;Mori H;Ihara Y;Yanagisawa M;Mosaki T;Hirokawa N
  19. J Neurochemistry v.59 Brain levels of microtubule-associated protein τ are elevated in Alzheimer's disease: A radioimmuno-slot-blot assay for nanograms of the protein Khatoon S;Grundke-Iqbal I;Iqbal K
  20. Brain v.87 Alzheimer's disease - an electron microscopical study Kidd M
  21. Science v.251 A68: A major subunit of paired helical filaments and derivatized forms of normal tau Lee VMY;Balin BJ;Otvos L, Jr;Trojanowski JQ
  22. J Am Chem Soc v.85 Solid phase peptide synthesis.Ⅰ.The synthesis of a tetrapeptide Merrifield RB
  23. J Biochem v.102 In vitro conditions for the self-polymerization of the microtubule-associated protein, tau factor Montejo de Garcini E;Avila J
  24. Neuroscience v.37 Characterization of tau protein present in microtubules and paired helical filaments of Alzheimer's disease patient's brain Nieto A;Montejo de Garcini E;Correas I;Avila J
  25. Molecular cloning: A laboratory manual Sambrook J;Fritsch EF;Maniatis T
  26. Biochemistry(2nd ed.) Stryer L
  27. J Am Chem Soc v.105 SN2 deprotection of synthetic peptides with a low concentration of HF in dimethyl sulfide: Evidence and application in peptide synthesis Tam JP;Heath WF;Merrifield RB
  28. Proc Natl Acad Sci USA v.72 A protein factor essential for microtubule assembly Weingarten MD;Lockwood AH;Hwo SY;Kirschner MW
  29. Pro Natl Acad Sci USA v.85 Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease Wischik CW;Novak M;Thogersen HC;Edwards PC;Runswick MJ;Jakes R;Walker JE;Milstein C;Roth M;Klug A
  30. J Neuropathol Exp Neurol v.43 Ultrastructure of paired helical filaments of Alzheimer's neurofibrillary tangle Wisniewski HM;Merz PA;Iqbal K
  31. J Neurol Sci v.27 Neuro-fibrillary tangles of paired helical filaments Wisniewski HM;Narany HK;Terry RD