Disease relevance of TEKT1

• Search for eukaryotic motility proteins in spirochetes: immunological detection of a tektin-like protein in Spirochaeta halophila [1].
• To continue testing, the SET proteins associated with eukaryotic motility (tektin, centrin and calmodulin) were sought in Spirochaeta halophila [1].
• The C tektin epitope was not detected in Escherichia coli [1].

High impact information on TEKT1

• Monoclonal antibodies specific for each of the flagellar tektins were prepared and used to determine whether structures similar to tektin filaments are present in cells lacking cilia or flagella [2].
• Cross-reactivity of antibodies specific for flagellar tektin and intermediate filament subunits [2].
• The proline content correlates well with the fact that tektin filaments have twice as much alpha-helical content as tubulin [3].
• With reverse-phase HPLC on a C18 column, using 6 M guanidine-HCl solubilization and a 0.1% trifluoroacetic acid/CH3CN gradient system (Stephens, R. E., 1984, J. Cell Biol. 90:37a [Abstr.]), the relatively less hydrophobic 51-kD tektin elutes at greater than 45% CH3CN, immediately followed by the 55-kD chain [3].
• Localization of tektin filaments in microtubules of sea urchin sperm flagella by immunoelectron microscopy [4].

Biological context of TEKT1

• A new member of the tektin gene family was cloned from the human fetal brain cDNA library [5].
• Included were a sequence conserved in the tektin B1 family, the TEKTIN2 motif, and the consensus sequence in the tektin protein family composed of nona-peptide [6].
• Transcriptional control of tektin A mRNA correlates with cilia development and length determination during sea urchin embryogenesis [7].
• The tektin polypeptide chains are divided into two major segments that have significant sequence homology to each other, both within a given tektin chain and between tektins A and B, indicative of gene duplication events [8].
• Synchronous expression with tektin and hepatocyte nuclear factor 3/forkhead homologue 4, down-regulation by interleukin-13, and its tissue distribution strongly suggested that CBE1 is associated with ciliated cells [9].

Anatomical context of TEKT1

• Tektin-t is a part of the tektin protein family, the members of which form filamentous polymers in the walls of ciliary and flagellar microtubules [6].
• The structural pattern of all three tektin polypeptides is similar to intermediate filament proteins [10].
• Molecular cloning of haploid germ cell-specific tektin cDNA and analysis of the protein in mouse testis [11].
• To determine the degree of the immunological relationship, tektin filaments and purified intermediate filaments from HeLa cells were cleaved with alpha-chymotrypsin and examined by quantitative immunoblot analysis [12].
• In the spirochetes, one tektin-like protein was detected as a band on Western blots (a C tektin.) An antibody made against Lytechinus pictus sperm tail axonemes, affinity-purified against the C tektin of another sea urchin, Stronglyocentrotus purpuratus, bound to a 30 kDa protein from Spirochaeta halophila [1].

Associations of TEKT1 with chemical compounds

• To investigate further the molecular mechanism for the regulation of tektin synthesis, tektin cDNA clones were used to assess mRNA levels during ciliogenesis, zinc-induced animalization, deciliation-induced regeneration and theophylline-induced elongation [7].
• Along each tektin rod cysteine residues occur with a periodicity of approximately 8 nm, coincident with the axial repeat of tubulin dimers in microtubules [10].
• Extraction of doublet microtubules from the sperm flagella of the sea urchin Strongylocentrotus purpuratus with sarkosyl (0.5%)-urea (2.5 M) yields a highly pure preparation of "tektin" filaments that we have previously shown to resemble intermediate filament proteins [4].

Other interactions of TEKT1

• A 480 A axial periodicity within these ribbons, revealed by scanning transmission electron microscopy, can be related to the structure of tektin, and may determine the large-scale structure of the axoneme in terms of the binding of dynein, nexin and radial spokes to the doublet microtubule [13].
• Although neither centrin nor calmodulin were detected, a 30 kDa tektin-like protein apparently is present in these spirochetes [1].

Analytical, diagnostic and therapeutic context of TEKT1

• High resolution two-dimensional tryptic peptide mapping reveals 63-67% coincidence among peptides of the 51-kD tektin chain and its 47- and 55-kD counterparts, greater than 70% coincidence between the 47- and 55-kD tektins, but little obvious similarity to either alpha- or beta-tubulin [3].
• Doublet microtubules were fractionated into tektin filaments and separated by SDS-PAGE into three major tektin polypeptide bands (Mr = 47, 51 and 55 (X 10(3)), which were used to immunize rabbits [14].
• Antibodies against each tektin (anti-tektins) were affinity-purified and then characterized by two-dimensional isoelectric focusing/SDS-PAGE immunoblotting and by immunofluorescence microscopy [14].
• Using a new antibody to tektin consensus peptide RPNVELCRD, well-characterized chain-specific antibodies and quantitative gel densitometry, tektins A, B and C were found to be present in equimolar amounts in Sarkosyl-urea-stable filaments [15].
• Western blot immunological detection techniques (for tektin and centrin) and two-dimensional gel analysis (for calmodulin) were used [1].

References