Tubulin Binding and Polymerization Promoting Properties of Tubulin Polymerization Promoting Proteins Are Evolutionarily Conserved
| Autor: | Péter Lőw, Tibor Szénási, Mauro Štifanić, Judit Oláh, Adél Szabó, Ferenc Orosz, Kinga Kovács |
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| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Protein family Nerve Tissue Proteins macromolecular substances Microtubules Biochemistry Protein Structure Secondary Conserved sequence Tubulin binding Evolution Molecular 03 medical and health sciences Protein structure Tubulin Microtubule Animals Amino Acid Sequence Peptide sequence Conserved Sequence biology Circular Dichroism Proteins biology.organism_classification INTRINSICALLY UNSTRUCTURED PROTEINS CIRCULAR-DICHROISM SECONDARY STRUCTURE RAT-BRAIN TPPP/P25 FAMILY PREDICTION DYNAMICS P25 OLIGODENDROCYTES Cell biology Suberites domuncula Microscopy Electron 030104 developmental biology biology.protein Suberites |
| Popis: | Tubulin polymerization promoting proteins (TPPPs) constitute a eukaryotic protein family. There are three TPPP paralogs in the human genome, denoted as TPPP1–TPPP3. TPPP1 and TPPP3 are intrinsically unstructured proteins (IUPs) that bind and polymerize tubulin and stabilize microtubules, but TPPP2 does not. Vertebrate TPPPs originated from the ancient invertebrate TPPP by two-round whole- genome duplication ; thus, whether the tubulin/microtubule binding function of TPPP1 and TPPP3 is a newly acquired property or was present in the invertebrate orthologs (generally one TPPP per species) has been an open question. To answer this question, we investigated a TPPP from a simple and early branching animal, the sponge Suberites domuncula. Bioinformatics, biochemical, immunochemical, spectroscopic, and electron microscopic data showed that the properties of the sponge protein correspond to those of TPPP1 ; namely, it is an IUP that strongly binds tubulin and induces its polymerization, proving that these features of animal TPPPs have been evolutionarily conserved. |
| Databáze: | OpenAIRE |
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