MicrotubulesBeta-tubulinMicrotubuleSubunitsHeterodimerProteinFtsZZinc-induced tubulin sheetsProteinsHeterodimersBindsCurvatureGTPaseHollowStructuralMoleculesGlobularKinesin-13PolymerizeAdjacentPolymerizationStructuresDimerTightlyCytoplasmBoundElectronConsistsStructureInteractionAlphaRapidlyEndsDrugsFormation
Microtubules22
- Alpha- and beta-tubulin, the main components of microtubules, have gained considerable interest because of their function and biophysical properties and has become the subject of intense study. (wikipedia.org)
- These compounds inhibit cell mitosis by binding to the protein tubulin in the mitotic spindle and preventing polymerization or depolymerization into the microtubules. (wikipedia.org)
- Microtubules are composed of two globular protein subunits, α- and β-tubulin. (wikipedia.org)
- Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division, it is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. (embl-heidelberg.de)
- mec-7 is a beta-tubulin gene required for the production of 15-protofilament microtubules in Caenorhabditis elegans. (wikidata.org)
- A basal body is a centriole , which is a cylinder-shaped structure composed of microtubules that in turn contain up to 13 protofilaments surrounding a hollow center. (sciencing.com)
- The gamma tubulin of an MTOC joins with other proteins to form ring complexes that provide a binding site for the microtubules. (sciencing.com)
- Microtubules are composed of alpha- and beta-tubulin subunits assembled into linear protofilaments. (camomienoteca.com)
- Microtubules are built through the lateral assembly of linear protofilaments formed through the head-to-tail association of tubulin dimers (1). (camomienoteca.com)
- Microtubules grow through the addition of tubulin dimers at their tips. (camomienoteca.com)
- Microtubules are formed from protein subunits called tubulin . (pediagenosis.com)
- The plant alkaloid colchicine binds to tubulin molecules and prevents the assembly of microtubules. (pediagenosis.com)
- The basic building block of microtubules is a heterodimer consisting of α- and β-tubulin . (wikilectures.eu)
- Microtubules are biopolymers that are composed of subunits made from an abundant globular cytoplasmic protein known as tubulin. (fsu.edu)
- These microtubules are formed via hierarchical self-assembly of globular proteins in nanometer size, tubulins (3), which grow into linear protofilaments. (lesvilains.com)
- This ring consists primarily of FtsZ, a tubulin-like GTPase, that assembles into protofilaments similar to those in microtubules but different in their suprastructures. (elsevierpure.com)
- Microtubules (MTs) are hollow cylindrical polymers composed of αβ-tubulin heterodimers that align head-to-tail in the MT wall, forming linear protofilaments that interact laterally. (huji.ac.il)
- The microtubules within these processes have a consistent 13-protofilament lattice and are tightly regulated with regard to their polarity orientation. (silverchair.com)
- Comparison of tubulin structures obtained in different states has led to a model in which the tubulin monomer undergoes a conformational switch between a "straight" form found in the walls of microtubules and a "curved" form associated with depolymerization, and it was proposed recently that this model may apply also to FtsZ. (proteopedia.org)
- Consequently, assembling tubulin in the formation of microtubules is a well-planned and regulated procedure. (risingacademy.org)
- In 1963, after the development of using glutaraldehyde as a fixative, the consistency and resolution of tubulin improved, and the term "microtubules" (MTs) was introduced (4-6) . (cytoskeleton.com)
- There are nine outside pairs of microtubules, known as doublets, and two centre singlet microtubules, each with 13 protofilaments, embedded in the ciliary matrix that fills each axoneme. (risingacademy.org)
Beta-tubulin8
- The three-dimensional structure of FtsZ issimilar to the structure of alpha- and beta-tubulin. (embl-heidelberg.de)
- Structure of the alpha beta tubulin dimer by electron crystallography. (embl-heidelberg.de)
- This simply means that the tubulin has a slightly different structure compared to alpha and beta tubulin, which allows it to function differently. (sciencing.com)
- Each proto filament is made up of Alpha and Beta tubulin and both subunits are covalently linked. (microbiologynotes.org)
- Alpha and beta tubulin are heterodimer and arranged in head to tail manner, which provide polarity to microtubule that means, at positive end beta tubulin is exposed and at negative end alpha subunits is exposed. (microbiologynotes.org)
- Each alpha and beta tubulin bind with GTP, but GTP found in beta tubulin can be hydrolyse during polymerization. (microbiologynotes.org)
- Each subunit of the microtubule is made of two slightly different but closely related simpler units called alpha -tubulin and beta -tubulin that are bound very tightly together to form heterodimers. (fsu.edu)
- This organization gives the structure polarity, with only the alpha -tubulin proteins exposed at one end and only beta -tubulin proteins at the other. (fsu.edu)
Microtubule14
- These data reveal that the microtubule depolymerization activity of kinesin-8 originates from conformational changes of its motor core that are amplified by dynamic contacts between its extended loop-2 and tubulin. (nature.com)
- On curved microtubule ends, loop-1 inserts into preceding motor domains, forming head-to-tail arrays of kinesin-8s that complement loop-2 contacts with curved tubulin and assist depolymerization. (nature.com)
- On straight tubulin protofilaments in the microtubule lattice, loop-2-tubulin contacts inhibit conformational changes in the motor core, but in the ADP-Pi state these contacts are relaxed, allowing neck-linker docking for motility. (nature.com)
- We propose that these tubulin shape-induced alternations between pro-microtubule-depolymerization and pro-motility kinesin states, regulated by loop-2, are the key to the dual activity of kinesin-8 motors. (nature.com)
- The addition of tubulin ligands can affect microtubule stability and function, including mitosis, cell motion and intracellular organelle transport. (wikipedia.org)
- These protofilaments form the backbone of the hollow, cylindrical microtubule which is about 25 nanometers in diameter and varies from 200 nanometers to 25 micrometers in length. (wikipedia.org)
- About 12-13 protofilaments arrange themselves in parallel to form a C-shaped protein sheet, which then curls around to give a pipe-like structure called the microtubule. (wikipedia.org)
- Lateral association of protofilaments forms the hollow cylindrical microtubule. (camomienoteca.com)
- Each microtubule consists of parallel protofilaments, each composed of α- and β-tubulin dimers. (pediagenosis.com)
- A microtubule is formed by a circular assembly of thirteen protofilaments. (wikilectures.eu)
- There are more than 100 tubulins in a microtubule with 13 protofilaments and 0.1 µm length. (ijnnonline.net)
- Tau family of proteins MAP-2 and MAP-4 having positively charged amino acids which binds to negative charged tubulin surface and stabilize the microtubule. (microbiologynotes.org)
- As a result, there are 13 protofilaments in each microtubule, each made up of dimers that run perpendicular to the tubule's long axis. (risingacademy.org)
- One full microtubule, known as the A sub-fibre, with all 13 protofilaments, may be found in each doublet. (risingacademy.org)
Subunits2
- The subunits are organized to form 13 parallel protofilaments that point the same direction. (fsu.edu)
- A repeating array of tubulin subunits makes up a microtubule's wall. (risingacademy.org)
Heterodimer2
- The alphabeta tubulin heterodimer is the structural subunit ofmicrotubules, which are cytoskeletal elements that are essential forintracellular transport and cell division in all eukaryotes. (embl-heidelberg.de)
- Although a construct of only the motor domain of kinesin 13 binds to every heterodimer of a tubulin ring, a construct containing the neck and the motor domain occupies alternate binding sites. (silverchair.com)
Protein9
- This arrangement results in the formation of long protein fibres called protofilaments. (wikipedia.org)
- Click on the protein counts, or double click on taxonomic names to display all proteins containing Tubulin domain in the selected taxonomic class. (embl-heidelberg.de)
- The protofilaments are polymers of the protein tubulin . (sciencing.com)
- The batch of protein passes Quality Control when a specific activity greater than 0.05 mol GTP / mol FtsZ / min is obtained in Protofilament Buffer. (cytoskeleton.com)
- FtsZ is a prokaryotic homologue of the eukaryotic cytoskeletal protein tubulin and plays a central role in prokaryotic cell division. (proteopedia.org)
- Chemically, they are composed of the protein components -tubulin (tubulin A) and -tubulin, which are two separate forms of protein (tubulin B), each of which has a mass of M.W. 55,000 daltons. (risingacademy.org)
- Other controlling variables in the in vivo polymerization of tubulin include calcium and calmodulin (an acidic protein with four Ca2+ binding sites). (risingacademy.org)
- Soon after, Hideo Mohri gave the colchicine-binding protein the official name of tubulin (11) . (cytoskeleton.com)
- One protein (flagellin), which bears no resemblance to tubulin or dynein, makes up the bacterial flagellum, a specialised component of the extracellular cell wall. (risingacademy.org)
FtsZ10
- This domain is found in all tubulin chains, as well as the bacterial FtsZ family of proteins. (embl-heidelberg.de)
- FtsZ and tubulin are GTPases, this entry is the GTPase domain. (embl-heidelberg.de)
- FtsZ is a GTPase with weak sequence homology to tubulins.The nature of FtsZ polymers in vivo is unknown, but FtsZ can form tubules,sheets and minirings in vitro. (embl-heidelberg.de)
- FtsZ (filamentation temperature-sensitive Z) is the bacterial homolog of tubulin that polymerizes into rings localized to cell-division sites, and the constriction of these rings drives cytokinesis. (nih.gov)
- The X-ray crystal structure reveals that MciZ binds to the C-terminal polymerization interface of FtsZ, the equivalent of the minus end of tubulin. (nih.gov)
- Using in vivo and in vitro assays and microscopy, we show that MciZ, at substoichiometric levels to FtsZ, causes shortening of protofilaments and blocks the assembly of higher-order FtsZ structures. (nih.gov)
- Just like eukaryotic tubulin, FtsZ polymerizes as well as binds and hydrolyzes GTP in a polymerization dependent manner. (cytoskeleton.com)
- The biological activity of FtsZ can be determined in two ways, first from its ability to efficiently polymerize into protofilaments and sheets in vitro in the presence of Mg 2+ and GTP, and secondly to hydrolyze GTP to GDP and Pi. (cytoskeleton.com)
- Both FtsZ and tubulin are known to pass through cycles of polymerization and depolymerization, but the structural mechanisms underlying this cycle remain to be determined. (proteopedia.org)
- FtsZ is a GTPase that is similar to the eukaryotic tubulins and is essential for cell division in. (systemsbiology.net)
Zinc-induced tubulin sheets2
- Here we present anatomic model of the alphabeta tubulin dimer fitted to a 3.7-A density mapobtained by electron crystallography of zinc-induced tubulin sheets. (embl-heidelberg.de)
- The structure of negatively stained zinc-induced tubulin sheets has been studied in projection by minimum beam microscopy and image processing. (escholarship.org)
Proteins5
- There are 39333 Tubulin domains in 39264 proteins in SMART's nrdb database. (embl-heidelberg.de)
- Taxonomic distribution of proteins containing Tubulin domain. (embl-heidelberg.de)
- The complete taxonomic breakdown of all proteins with Tubulin domain is also avaliable . (embl-heidelberg.de)
- The tubulin proteins in flagella and cilia are of the alpha and beta variety. (sciencing.com)
- These are unbranched tubules with a solid wall (5 nm thick) composed of tubulin proteins. (wikilectures.eu)
Heterodimers2
- While stepping, ATP hydrolysis is coupled to an 8 nm center-of-mass displacement (Figure 2a) [BNID 112201 ], the distance between adjacent tubulin heterodimers. (harvard.edu)
- The 8.2 nm repeat arises from the arrangement of heterodimers in the protofilaments, and is the first observation of such a repeat in sheet aggregates. (escholarship.org)
Binds1
- The first known compound which binds to tubulin was colchicine, it was isolated from the autumn crocus, Colchicum autumnale, but it has not been used for cancer treatment. (wikipedia.org)
Curvature2
- we report a detailed dissection of the three- dimensional organisation of the conoid and show there is high curvature of the tubulin-containing fibres that might be linked to the unusual comma-shaped arrangement of protofilaments. (brookes.ac.uk)
- We propose a new model in which lateral interactions help determine the curvature of protofilaments. (proteopedia.org)
GTPase1
- GTPase activity is determined in a "Protofilament Buffer" by measuring the Pi released over time by using the MESEG phosphate detection kit (Cat# BK052 ) or an endpoint assay (Cat. (cytoskeleton.com)
Hollow1
- In coccidian apicomplexans there is an additional tubulin-containing hollow barrel structure, the conoid, which provides a structural gateway for this specialised apical secretion. (brookes.ac.uk)
Structural2
- The aim of this study is to develop a molecular dynamics model (MDM), finite element model (FEM) and structural mechanics beam model (SMBM) for tubulins of protofilament (PF). (techscience.com)
- It has been shown to be a bacterial homolog of eukaryotic tubulin, based both on a low sequence identity and a striking structural similarity (2). (cytoskeleton.com)
Molecules2
- Tubulin binding molecules have generated significant interest after the introduction of the taxanes into clinical oncology and the general use of the vinca alkaloids. (wikipedia.org)
- Polymerization of these dimer molecules (with the participation of GTP) creates spirally arranged protofilaments , on which we distinguish (+) and (−) ends. (wikilectures.eu)
Globular1
- A microtubule's wall is composed of 13 protofilaments, which have a diameter of 4 to 5 nm and are globular in shape. (risingacademy.org)
Kinesin-132
- These results indicate that the second head of dimeric kinesin 13 does not have access to adjacent binding sites on the curved protofilament and suggest that the neck alone is sufficient to obstruct access. (silverchair.com)
- Together, these data suggest a model for kinesin 13 depolymerization in which increased efficiency is achieved by binding of one kinesin 13 molecule to adjacent protofilaments. (silverchair.com)
Polymerize1
- During the reassembly process the tubulin dimers polymerize in an end-to-end fashion to form protofilaments. (pediagenosis.com)
Adjacent1
- During polymerization, the dimers are organized in such a way that α-tubulin is always adjacent to β-tubulin. (wikilectures.eu)
Polymerization1
- This pool is used in the polymerization process for reassembly of the protofilaments. (pediagenosis.com)
Structures1
- These structures are unique because they consist of the gamma form of tubulin. (sciencing.com)
Dimer1
- The tubulin hetero-dimers arrange themselves in a head to tail manner with the α-subunit of one dimer coming in contact with the β-subunit of the other. (wikipedia.org)
Tightly1
- One molecule of GTP is tightly bound to the α-tubulin and is non-exchangeable whereas the other GTP molecule is bound to β-tubulin and can be easily exchanged with guanosine diphosphate (GDP). (wikipedia.org)
Cytoplasm1
- During the disassembly process, the tubulin dimers dissociate from the protofilaments and form a pool of free tubulin in the cytoplasm. (pediagenosis.com)
Bound1
- An important gap in our understanding of the kinesin-8 depolymerization mechanism is the lack of a kinesin-8 structure bound to curved tubulin. (nature.com)
Electron1
- The first images of tubulin within the cell began to be observed in the 1950s and 1960s via transmission electron microscopy (1) . (cytoskeleton.com)
Consists1
- Our in vitro reconstitution experiments suggest that the Z-ring consists of dynamic protofilament bundles in which monomers constantly are exchanged throughout, stochastically creating protofilament ends along the length of the filament. (elsevierpure.com)
Structure3
- Figure (a) shows a typical sheet image, displaying the characteristic and prominent protofilament structure. (escholarship.org)
- 4) Subsequently, these protofilaments are assembled together to build a multi-stranded tubular structure with a length over tens of micrometers. (lesvilains.com)
- However, initial fixation methods at that time did not preserve the tubulin structure for it to be observed consistently. (cytoskeleton.com)
Interaction1
- The first and most important step for this process is to obtain the interaction force between tubulins. (ijnnonline.net)
Alpha2
- The alpha- and beta-tubulins share 40% amino-acidsequence identity, both exist in several isotype forms, and both undergo avariety of posttranslational modifications. (embl-heidelberg.de)
- Turnover of the carboxy-terminal tyrosine of alpha-tubulin and means of reaching elevated levels of detyrosination in living cells. (sysy.com)
Rapidly1
- The two ends are not equal, the α-tubulin ringed (-)end is less dynamic while the more dynamic β-tubulin ringed (+) end grows and shortens more rapidly. (wikipedia.org)
Ends1
- Most kinesins walk along the MT, but class 13 kinesins instead uniquely recognize MT ends and depolymerize MT protofilaments. (silverchair.com)
Drugs1
- Tubulin inhibitors are chemotherapy drugs that interfere directly with the tubulin system, which is in contrast to those chemotherapy drugs acting on DNA. (wikipedia.org)
Formation1
- Tubulin detyrosination promotes monolayer formation and apical trafficking in epithelial cells. (sysy.com)