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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1991-10-31
|
| pubmed:abstractText |
We describe the presence of alpha-tubulin and MAP2 acetyltransferase activities in mouse brain. The enzyme(s) copurified with microtubules through two cycles of assembly-disassembly. Incubation of microtubule proteins with [3H]acetyl CoA resulted in a strong labeling of both alpha-tubulin and MAP2. To determine the site of the modification, tubulin was purified and digested with Glu-C endoproteinase. A unique radioactive peptide was detected and purified by HPLC. Edman degradation sequencing showed that this peptide contained epsilon N-acetyllysine at position 40 of the alpha-tubulin molecule. This result demonstrates that mouse brain alpha-tubulin was acetylated at the same site as in Chlamydomonas. Isoelectric focusing analysis showed that acetylated alpha-tubulin was resolved into five isoelectric variants, denoted alpha 3 and alpha 5 to alpha 8. This heterogeneity is not due to acetylation of other sites but results from a single acetylation of Lys40 of an heterogeneous population of alpha-tubulin isoforms. These isoforms are produced by posttranslational addition of one to five glutamyl units. Thus, neuronal alpha-tubulin is extensively modified by a combination of modifications including acetylation, glutamylation, tyrosylation, and other yet unknown modifications.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamates,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tubulin,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-tubulin acetylase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0730-2312
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
46
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
134-42
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:1680872-Acetylation,
pubmed-meshheading:1680872-Acetyltransferases,
pubmed-meshheading:1680872-Amino Acid Sequence,
pubmed-meshheading:1680872-Animals,
pubmed-meshheading:1680872-Astrocytes,
pubmed-meshheading:1680872-Brain,
pubmed-meshheading:1680872-Brain Chemistry,
pubmed-meshheading:1680872-Cells, Cultured,
pubmed-meshheading:1680872-Chlamydomonas,
pubmed-meshheading:1680872-Chromatography, High Pressure Liquid,
pubmed-meshheading:1680872-Glutamates,
pubmed-meshheading:1680872-Glutamic Acid,
pubmed-meshheading:1680872-Mice,
pubmed-meshheading:1680872-Microtubule-Associated Proteins,
pubmed-meshheading:1680872-Molecular Sequence Data,
pubmed-meshheading:1680872-Neurons,
pubmed-meshheading:1680872-Protein Processing, Post-Translational,
pubmed-meshheading:1680872-Tubulin
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
A combination of posttranslational modifications is responsible for the production of neuronal alpha-tubulin heterogeneity.
|
| pubmed:affiliation |
Laboratoire de Biochimie Cellulaire, Collège de France, Paris.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|