Biochemistry: Tubulin polyglutamylase enzymes are members of the TTL domain protein family

Science

Volumn 308, Issue 5729, 2005, Pages 1758-1762

  Janke, Carsten ^a   Rogowski, Krzysztof ^b   Wloga, Dorota ^b   Regnard, Catherine ^c   Kajava, Andrey V ^a   Strub, Jean Marc ^d   Temurak, Nevzat ^a   Van Dijk, Juliette ^a   Boucher, Dominique ^a   Van Dorsselaer, Alain ^d   Suryavanshi, Swati ^b   Gaertig, Jacek ^b   Eddé, Bernard ^a,e  

^a CNRS   (France)

^b UNIVERSITY OF GEORGIA   (United States)

^c UNIVERSITY OF MUNICH   (Germany)

^d UNIVERSITÉ DE STRASBOURG   (France)

^e SORBONNE UNIVERSITÉ   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CATALYST ACTIVITY; PROTEINS; SUBSTRATES;

MICROTUBULES; POLYGLUTAMYLATION; SUBCELLULAR LOCALIZATION; TUBULIN TYROSINE LIGASE-LIKE (TTLL);

ENZYMES;

ENZYME; PROTEIN; TUBULIN; TUBULIN POLYGLUTAMYLASE; TUBULIN TYROSINE LIGASE LIKE PROTEIN; UNCLASSIFIED DRUG; HYBRID PROTEIN; PEPTIDE SYNTHASE; POLYGLUTAMIC ACID; PROTEIN SUBUNIT; TTLL1 PROTEIN, HUMAN; TTLL1 PROTEIN, MOUSE;

BIOCHEMISTRY;

ARTICLE; CATALYSIS; CHEMICAL MODIFICATION; ENZYME LOCALIZATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; LIGATION; MICROTUBULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; TETRAHYMENA THERMOPHILA; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; BRAIN; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; EUKARYOTIC FLAGELLUM; GENETICS; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; MOUSE; MOVEMENT (PHYSIOLOGY); PHYLOGENY; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN MOTIF;

PROTISTA; TETRAHYMENA THERMOPHILA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BRAIN; CATALYTIC DOMAIN; CILIA; HUMANS; MICE; MICROTUBULES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOVEMENT; PEPTIDE SYNTHASES; PHYLOGENY; POLYGLUTAMIC ACID; PROTEIN CONFORMATION; PROTEIN SUBUNITS; RECOMBINANT FUSION PROTEINS; SUBSTRATE SPECIFICITY; TETRAHYMENA THERMOPHILA; TUBULIN;

EID: 20544457358     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1113010     Document Type: Article

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28. Supported by Association de la Recherche contre le Cancer award ARC 5859 (B.E.), Fondation pour la Recherche Médicale award INE20021108027/1 (C.J.), NSF award MBC-0235826 (J.G.), and EMBO long-term fellowship ALTF 387-2001 (C.J.). Preliminary sequence data for Tetrahymena thermophila were obtained from The Institute for Genomic Research. We thank E. Desbruyères, G. Herrada-Aldrian, J. M. Donnay, A. Bernet, and G. Rabeharivelo for technical assistance; P. Chaussepied, J. Frankel, M. Gorovsky, E. Kipreos, and M. Fechheimer for helpful comments; R. Melki for antibody to Arp1; S. Dettwiler and W. Keller for antibody to CF Im25; M. Gorovsky for antibodies polyG and polyE; K. Weber and S. Westermann for mAb ID5; and J. Frankel for mAb 12G10. Molecular interaction data have been deposited in the Biomolecular Interaction Network Database with accession code 295280.