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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

mRNA specific to cDNA clone pLK109 is present in Dictyostelium discoideum spores, increases about two- to threefold at 0.5 to 1 h during spore germination, and then rapidly decreases. The mRNA is not detectable in vegetative cells or in early multicellular development on filters, but is present late during development, approximately at the time of sporulation. 109 mRNA in spores is 700 nucleotides in length but this is processed during germination by shortening of the poly(A) tail to about 600 nucleotides at 1 to 1.5 hours. pLK109 is a member of a multigene family containing three separate genes, and we have isolated and sequenced all of them. All three sequences code for deduced proteins of 127 amino acid residues, with only a few amino acid differences among them. Gene 1 represents the "transcribed" gene, since all 33 cDNAs we isolated are identical with the cDNA pLK109 and the coding region of this gene. Other open reading frames are in close proximity to each of the 109 sequences. About 200 base-pairs 3' to the gene 1 109 sequence is an open reading frame in the opposite orientation. Gene 2 fragment contains a sequence that codes for a protein similar to trypanosome alpha-tubulin 728 base-pairs 5' to the 109 sequence. Gene 3 fragment possesses two additional putative coding regions, one 5' and another 3' to the 109 gene. There is a remarkable similarity between the 5' upstream regions of all three genes. Each possesses a normal Dictyostelium TATA box and the usual T stretch. In addition, there are many other portions of about 400 to 500 base-pairs of the 5' regions that are either identical for long stretches or very similar.
J Mol Biol 1989 Jan 05
PMID:Organization of a gene family developmentally regulated during Dictyostelium discoideum spore germination. 292 9

The tubulins of Brugia malayi and B. pahangi were similar with respect to concentration (mg tubulin per mg soluble protein), electrophoretic and isoelectric mobility, reaction in Western blots with anti-tubulin monoclonal antibodies, and isoform patterns. Tubulin was estimated to account for 2.8% and 2.9% of soluble protein in B. malayi and B. pahangi extracts, respectively. Tubulins from Brugia nematodes have been partially purified by polylysine agarose chromatography and with taxol. Western blots with alpha- and beta-tubulin monoclonal antibodies confirmed the presence of tubulin. The mobility of Brugia tubulins on sodium dodecyl sulfate polyacrylamide gel electrophoresis was very similar to that of N. brasiliensis and rat brain tubulins. The isoelectric range for Brugia alpha- and beta-tubulin isoforms was pH 5.4-4.7. Western blots with anti-tubulin monoclonal antibodies revealed 4-5 isoforms of alpha-tubulin and 4-5 isoforms of beta-tubulin for Brugia nematodes.
Mol Biochem Parasitol 1989 Jan 15
PMID:Characterization of tubulin from Brugia malayi and Brugia pahangi. 292 43

In both clam oocytes and sea urchin eggs, fertilization triggers the synthesis of a set of proteins specified by stored maternal mRNAs. One of the most abundant of these (p41) has a molecular weight of 41,000. This paper describes the identification of p41 as the small subunit of ribonucleotide reductase, the enzyme that provides the precursors necessary for DNA synthesis. This identification is based mainly on the amino acid sequence deduced from cDNA clones corresponding to p41, which shows homology with a gene in Herpes Simplex virus that is thought to encode the small subunit of viral ribonucleotide reductase. Comparison with the B2 (small) subunit of Escherichia coli ribonucleotide reductase also shows striking homology in certain conserved regions of the molecule. However, our attention was originally drawn to protein p41 because it was specifically retained by an affinity column bearing the monoclonal antibody YL 1/2, which reacts with alpha-tubulin (Kilmartin, J. V., B. Wright, and C. Milstein, 1982, J. Cell Biol., 93:576-582). The finding that this antibody inhibits the activity of sea urchin embryo ribonucleotide reductase confirmed the identity of p41 as the small subunit. The unexpected binding of the small subunit of ribonucleotide reductase can be accounted for by its carboxy-terminal sequence, which matches the specificity requirements of YL 1/2 as determined by Wehland et al. (Wehland, J., H. C. Schroeder, and K. Weber, 1984, EMBO [Eur. Mol. Biol. Organ.] J., 3:1295-1300). Unlike the small subunit, there is no sign of synthesis of a corresponding large subunit of ribonucleotide reductase after fertilization. Since most enzymes of this type require two subunits for activity, we suspect that the unfertilized oocytes contain a stockpile of large subunits ready for combination with newly made small subunits. Thus, synthesis of the small subunit of ribonucleotide reductase represents a very clear example of the developmental regulation of enzyme activity by control of gene expression at the level of translation.
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PMID:The small subunit of ribonucleotide reductase is encoded by one of the most abundant translationally regulated maternal RNAs in clam and sea urchin eggs. 298 74

Two alpha-tubulin genes from the budding yeast Saccharomyces cerevisiae were identified and cloned by cross-species DNA homology. Nucleotide sequencing studies revealed that the two genes, named TUB1 and TUB3, encoded gene products of 447 and 445 amino acids, respectively, that are highly homologous to alpha-tubulins from other species. Comparison of the sequences of the two genes revealed a 19% divergence between the nucleotide sequences and a 10% divergence between the amino acid sequences. Each gene had a single intervening sequence, located at an identical position in codon 9. Cell fractionation studies showed that both gene products were present in yeast microtubules. These two genes, along with the TUB2 beta-tubulin gene, probably encode the entire complement of tubulin in budding yeast cells.
Mol Cell Biol 1986 Nov
PMID:Two functional alpha-tubulin genes of the yeast Saccharomyces cerevisiae encode divergent proteins. 302 10

Thirteen monoclonal antibodies (MAbs) specific for the membrane of live Trypanosoma cruzi have been obtained from BALB/c infected mice. Most of them had greater avidity for intact than for disrupted parasites. According to the staining by indirect immunofluorescence of the different live developmental stages of the parasite the MAbs could be divided into several groups. Three of them were trypomastigote specific, one amastigote-specific and two epimastigote-specific. The rest reacted with either all stage forms or with various combinations of the different stages. However, despite the fact that they seemed to correspond to stage-specific antibodies, ten of them reacted with the same 55/50 kDa antigen by immunoblotting. Similarly, a 55 kDa protein was immunoprecipitated from these MAbs. By contrast, a single band or a dimer of about 25 kDa was the predominant antigen(s) immunoprecipitated by the same MAbs in absence of protease inhibitors. This smaller protein may arise from proteolysis of the 55 kDa band. This protein is related to tubulin since tubulin (a 55 kDa protein) but not other cytoskeleton proteins blocked the binding of these MAbs to T. cruzi, and some MAbs react with pig alpha-tubulin by immunoblotting.
Mol Biochem Parasitol 1988 Jun
PMID:A tubulin-related 55 kilodalton surface antigen recognized by different Trypanosoma cruzi stage-specific monoclonal antibodies from infected mice. 304 40

It has been established that the 90-kilodalton murine heat shock protein, hsp90, is associated with the untransformed, non-DNA-binding form of the glucocorticoid receptor in L cell cytosol. In this work, we show that incubation of L cell cytosol with Affi-Gel-coupled monoclonal antibodies directed against either alpha-tubulin alone or both alpha- and beta-tubulin results in the immune-specific adsorption of hsp90 identified by Western blotting with the AC88 monoclonal antibody. Similarly, the AC88 antibody, which is specific for hsp90, causes the immune-specific isolation of both alpha- and beta-tubulin from hypotonic cytosol. The distribution of hsp90 in cultured Potorous tridactylis kidney cells was examined by indirect immunofluorescence using the AC88 monoclonal as primary antibody. In interphase cells, AC88-dependent fluorescence was distributed like antitubulin antibody-dependent fluorescence in a fibrillar array located in the cytoplasm and around the periphery of the nucleus. In cells undergoing mitosis, AC88 fluorescence was located in the mitotic spindle. These observations suggest that a significant portion of hsp90 is associated with a tubulin-containing complex both in a hypotonic cytosol preparation from mouse fibroblasts and in intact marsupial kidney epithelial cells. The distribution of AC88 fluorescence in interphase Potorous tridactylis kidney cells is similar to the distribution of glucocorticoid receptor demonstrated by Wikstrom, A. C., Bakke, O., Okret, S., Bronnegard, M., and Gustafsson, J. A in rat hepatoma and human uterine cells.
Mol Endocrinol 1988 Aug
PMID:Evidence that the 90-kilodalton heat shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells. 306 85

Tubulin can be posttranslationally modified at the carboxyl terminus of the alpha-subunit by the addition or release of a tyrosine residue. These reactions involve two enzymes, tubulin: tyrosine ligase and tubulin carboxypeptidase. The tyrosine incorporation reaction has been described mainly in nervous tissue but it has also been found in a great variety of tissues and different species. Molecular aspects of the reactions catalyzed by these enzymes are at present well known, especially the reaction carried out by the ligase. Several lines of evidence indicate that assembled tubulin is the preferred substrate of the carboxypeptidase, whereas nonassembled tubulin is preferred by the ligase. Apparently this posttranslational modification does not affect the capacity of tubulin to form microtubules but it generates microtubules with different degrees of tyrosination. Variation in the content of the carboxyterminal tyrosine of alpha-tubulin as well as changes in the activity of the ligase and the carboxypeptidase are manifested during development. Changes in the cellular microtubular network modify the turnover of the carboxyterminal tyrosine of alpha-tubulin. Different subsets of microtubules with different degrees of tyrosination have been detected in interphase cells and during the mitotic cycle. Data from biochemical, immunological, and genetic studies have been compiled in this review; these are presented, with pertinent comments, with the hope of facilitating the comprehension of this particular aspect of the microtubule field.
Mol Neurobiol 1988
PMID:Posttranslational tyrosination/detyrosination of tubulin. 307 15

Castration of an adult male rat results in the rapid regression of the ventral prostate gland. Most of the acinar epithelial cells lining the ducts of the gland will die during the first 5 days after androgen withdrawal. The molecular events which accompany the death of these cells were studied by examining RNA isolated from ventral prostate glands of normal and from a sequential 24-h series of castrate rats. These RNAs were analyzed by Northern blot methods to quantify the expression of growth-related (c-fos, c-myc, and heat shock 70K) and cell maintenance (alpha-tubulin) genes during prostatic regression. Each of these genes showed a bimodal pattern of expression. Within the first few days after castration, transcript levels decline; whereas later, during the most active period of cell death, their expression was transiently induced. Levels of mature c-myc, and alpha-tubulin transcripts increased approximately 6- to 8-fold on the third day after castration, while transcripts encoding hsp 70-related genes increased greater than 6-fold on the fourth day after castration. Further analysis of RNA extracted from regressing ventral prostate glands at sequential 12-h intervals after castration showed that the c-fos gene was induced at 36 h, earlier than c-myc, alpha-tubulin, and hsp 70.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Endocrinol 1988 Jul
PMID:Cascade induction of c-fos, c-myc, and heat shock 70K transcripts during regression of the rat ventral prostate gland. 313 56

Macronuclear DNA of the ciliate Tetrahymena pyriformis contains only one size class of fragments coding for alpha-tubulin, alpha TT. We have isolated alpha TT from a partial plasmid library, using Chlamydomonas reinhardtii alpha-tubulin gene as a probe. This gene as well as the two beta-tubulin genes, beta TT1 and beta TT2, have been sequenced. None of these genes contains introns and all use TGA as the stop codon. In the coding region of the two beta-tubulin genes, there are several TAA and TAG stop codons that probably code for glutamine. The codon usage is very biased. Regions flanking the tubulin coding sequences are A + T-rich (75%) and quite different among themselves. In these regions there are several putative transcription-regulatory sequences. Nuclear transcripts begin and terminate at multiple sites. The beta-tubulin proteins differ only in two amino acid residues. Primary structure of Tetrahymena tubulins as well as their hydropathy indexes show a high degree of homology with tubulins from other organisms. Two-dimensional electrophoretic analysis of the ciliary tubulins shows the presence of eight alpha-tubulins and four beta-tubulins. The alpha-tubulins migrate faster than the beta-tubulins, in contrast with what happens with brain tubulins. We suggest that there are several alpha- and beta-tubulin isoforms and the migratory inversion observed may be due to post-translational modifications.
J Mol Biol 1988 Aug 05
PMID:Sequence of one alpha- and two beta-tubulin genes of Tetrahymena pyriformis. Structural and functional relationships with other eukaryotic tubulin genes. 313 85

Southern analysis of Volvox genomic DNA revealed two genes homologous to Chlamydomonas reinhardtii alpha-tubulin cDNA. Restriction fragment length polymorphism analysis indicated that the two genes are not genetically linked. Clones representing one of the alpha-tubulin genes have been isolated from a genomic library of Volvox carteri f. nagariensis. A 3153 bp BamHI fragment containing the entire alpha-tubulin gene (1802 bp) plus 707 bp of the 5'- and 644 bp of the 3'-untranslated regions has been sequenced, revealing the following features: (1) the derived alpha-tubulin primary structure of 451 amino acids is highly conserved, differing in two residues from the alpha 1- and in two additional residues from the alpha 2-tubulin of C. reinhardtii; (2) in comparison to the C. reinhardtii genes, the Volvox alpha-tubulin gene contains a third intron; positions of the other two introns are precisely conserved; (3) codon usages are biased towards G or C, and against A, in the third position; 19 codons are absent from the alpha-tubulin coding sequence, and 5 of these are not used in any of 7 compiled Volvox genes; (4) transcription begins with an A, 30 bp downstream of the putative TATA box; upstream of the TATA box is a 14 bp sequence similar to consensus sequences found in all 4 C. reinhardtii tubulin genes and believed to regulate promoter function.
Mol Gen Genet 1988 Aug
PMID:Organization and structure of Volvox alpha-tubulin genes. 318 11


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