Inhibition of tubulin self-assembly in vitro by fluorodinitrobenzene. 1981

Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes

The self-assembly of bovine brain tubulin into microtubules is inhibited by low molar ratios of 1-fluoro-2,4-dinitrobezene (FDNB). Binding studies using [14C]FDNB indicate that the incorporation of between one and two dinitrophenyl groups is sufficient to inhibit assembly completely, although more dinitrophenyl groups can be incorporated using higher FDNB/tubulin ratios. Dinitrophenyltubulin, under assembly conditions, tends to assemble into amorphous aggregates. Thiolysis by 2-mercaptoethanol removes the dinitrophenyl moieties. Paper chromatography and high-voltage electrophoresis of acid-hydrolyzed modified tubulin containing one dinitrophenyl group identified the residue as S-dinitrophenylcysteine. The beta-monomer of tubulin is preferentially modified at low FDNB/tubulin ratios. The reaction with FDNB is greatly reduced when tubulin is in polymerized form. FDNB reduces the colchicine binding activity but does not affect the Mg(II) content of the protein.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D009578 Nitrobenzenes BENZENE derivatives carrying nitro group substituents.
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D001921 Brain The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM. Encephalon
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D004139 Dinitrofluorobenzene Irritants and reagents for labeling terminal amino acid groups. DNFB,Fluorodinitrobenzene,1-Fluoro-2,4-dinitrobenzene,1 Fluoro 2,4 dinitrobenzene
D004140 Dinitrophenols Organic compounds that contain two nitro groups attached to a phenol.
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D014404 Tubulin A microtubule subunit protein found in large quantities in mammalian brain. It has also been isolated from SPERM FLAGELLUM; CILIA; and other sources. Structurally, the protein is a dimer with a molecular weight of approximately 120,000 and a sedimentation coefficient of 5.8S. It binds to COLCHICINE; VINCRISTINE; and VINBLASTINE. alpha-Tubulin,beta-Tubulin,delta-Tubulin,epsilon-Tubulin,gamma-Tubulin,alpha Tubulin,beta Tubulin,delta Tubulin,epsilon Tubulin,gamma Tubulin

Related Publications

Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
November 1978, Biochimica et biophysica acta,
Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
June 1981, Biochemistry,
Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
April 2007, Proteins,
Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
March 1990, FEBS letters,
Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
May 1976, Biochemical and biophysical research communications,
Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
March 1996, Biochemistry,
Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
June 1982, Nature,
Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
September 1987, Biochemistry,
Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
April 1982, Biochemical and biophysical research communications,
Y C Lee, and R A Yaple, and R Baldridge, and M Kirsch, and R H Himes
February 1986, The Journal of biological chemistry,
Copied contents to your clipboard!