Publikationsdatum:
2005-05-14
Beschreibung:
Polyglutamylation of tubulin has been implicated in several functions of microtubules, but the identification of the responsible enzyme(s) has been challenging. We found that the neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase-like (TTLL) protein, TTLL1. TTLL1 is a member of a large family of proteins with a TTL homology domain, whose members could catalyze ligations of diverse amino acids to tubulins or other substrates. In the model protist Tetrahymena thermophila, two conserved types of polyglutamylases were characterized that differ in substrate preference and subcellular localization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janke, Carsten -- Rogowski, Krzysztof -- Wloga, Dorota -- Regnard, Catherine -- Kajava, Andrey V -- Strub, Jean-Marc -- Temurak, Nevzat -- van Dijk, Juliette -- Boucher, Dominique -- van Dorsselaer, Alain -- Suryavanshi, Swati -- Gaertig, Jacek -- Edde, Bernard -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1758-62. Epub 2005 May 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Recherches de Biochimie Macromoleculaire, CNRS, 34293 Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15890843" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Amino Acid Motifs
;
Amino Acid Sequence
;
Animals
;
Binding Sites
;
Brain/enzymology
;
*Catalytic Domain
;
Cilia/physiology
;
Humans
;
Mice
;
Microtubules/metabolism
;
Models, Molecular
;
Molecular Sequence Data
;
Movement
;
Peptide Synthases/*chemistry/genetics/isolation & purification/*metabolism
;
Phylogeny
;
Polyglutamic Acid/*chemistry/genetics/isolation & purification/*metabolism
;
Protein Conformation
;
Protein Subunits/chemistry/isolation & purification/metabolism
;
Recombinant Fusion Proteins/metabolism
;
Substrate Specificity
;
Tetrahymena thermophila/*enzymology/genetics/metabolism
;
Tubulin/*chemistry/genetics/isolation & purification/*metabolism
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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