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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1999-11-1
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pubmed:abstractText |
The minimal sequence requirement of Crithidia tubulin polyglutamylase is already fulfilled by tubulin-related peptides carrying a free alpha-carboxylate on a glutamic acid residue. Since the product of each glutamylation step fulfills the substrate requirements necessary for the next cycle, very long side chains are generated with brain tubulin as a substrate. Up to 70 mol of glutamic acid was incorporated per alphabeta-heterodimer. We speculate that the strict choice of a particular glutamate residue for the formation of the isopeptide bond initiating a novel side chain is made by a tubulin monoglutamylase which requires the entire tubulin as substrate.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
459
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
90-4
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pubmed:dateRevised |
2007-4-27
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pubmed:meshHeading |
pubmed-meshheading:10508923-Amino Acid Sequence,
pubmed-meshheading:10508923-Animals,
pubmed-meshheading:10508923-Brain,
pubmed-meshheading:10508923-Crithidia fasciculata,
pubmed-meshheading:10508923-Immunoblotting,
pubmed-meshheading:10508923-Molecular Sequence Data,
pubmed-meshheading:10508923-Peptide Synthases,
pubmed-meshheading:10508923-Peptides,
pubmed-meshheading:10508923-Polyglutamic Acid,
pubmed-meshheading:10508923-Sequence Homology, Amino Acid,
pubmed-meshheading:10508923-Substrate Specificity,
pubmed-meshheading:10508923-Tubulin
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pubmed:year |
1999
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pubmed:articleTitle |
Synthetic peptides identify the minimal substrate requirements of tubulin polyglutamylase in side chain elongation.
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pubmed:affiliation |
Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Am Fassberg 11, 37077, Goettingen, Germany.
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pubmed:publicationType |
Journal Article
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