Cloning and expression of chicken erythrocyte transglutaminase.

Weraarchakul-Boonmark, N.; Jeong, Je‐Myung; Murthy, S. N. Prasanna; Engel, James Douglas; Lóránd, L.

doi:10.1073/pnas.89.20.9804

Cited by 32 publications

(23 citation statements)

References 44 publications

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“…Monospecific anti-(nTG-M) Ig (1.9 lgAEmL )1 ), which had been preincubated with the antigenic peptide (1.1 lgAEmL )1 of affinity-purified Ig), was used as the negative control. The secondary antibody was [5], chicken erythrocyte TG (cEry) [30], Limulus hemocyte TG (lHem) [31], human keratinocyte TG (hKer) [3], human prostate TG (hPro) [6], and nTG are shown using the single letter amino acid codes. Gaps have been inserted to achieve maximum similarity.…”

Section: Immunofluorescence Microscopymentioning

confidence: 99%

“…Neither a polyadenylation signal (AATAAA) nor a poly(A) + tail was found in the 540-bp untranslated region following the termination codon (TAA), suggesting that the cDNA might not be full-length. Figure 2B shows the alignment of the deduced aminoacid sequence with those of the other known TGs from various species [2,3,5,6,30,31]. The predicted protein exhibited 33-41% identity with other TGs.…”

Section: R E S U L T S Molecular Cloning Of a Pectinifera Transglutamentioning

confidence: 99%

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Molecular characterization of a novel nuclear transglutaminase that is expressed during starfish embryogenesis

Sugino¹,

Terakawa²,

Yamasaki³

et al. 2002

Eur J Biochem

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We report the constitution and molecular characterization of a novel transglutaminase (EC 2.3.2.13) that starts to accumulate specifically in the nucleus in the starfish (Asterina pectinifera) embryo after progression through the early blastula stage. The cDNA for the nuclear transglutaminase was cloned and the cDNA-deduced sequence defines a single open reading frame encoding a protein with 737 amino acids and a predicted molecular mass of 83 kDa. A comparison of this transglutaminase with other members of the gene family revealed an overall sequence identity of 33-41%. A special sequence feature of this transglutaminase, which is not found in other transglutaminases, is the presence of nuclear localization signal-like sequences in the N-terminal region.Microinjection of hybrid constructs that encode the N-terminal segment fused to reporter proteins into the germinal vesicle of an oocyte produced chimeric proteins by transcription-coupled translation. It was found that the N-terminal segment alone was sufficient to effect nuclear accumulation of an otherwise cytoplasmic protein. These results suggest that the nuclear accumulation of the transglutaminase may play an important role in nuclear remodeling during early starfish embryogenesis.Keywords: transglutaminase; nucleus; starfish; embryo; cloning.The class of enzymes that are commonly referred to as transglutaminases (TG) (EC 2.3. Recent findings have shown that, apart from their protein modifying capabilities, tissue TG is also able to function as a component of the signal-transducing G protein complex [7]. The cDNA of G ha , involved in the transmission of adrenergic stimuli, is identical to that of tissue TG of human endothelial cells [7]. Tissue TG is localized mainly in the cytosol, but detectable tissue TG expression has been reported in the nucleus [8][9][10]. However, TG activity in the nucleus and the mechanisms of its translocation is not well understood, and nucleus-specific TG has not been reported.It is accepted that many proteins are able to cross nuclear membranes and accumulate against gradients to concentrate in the nucleus [11,12]. The nuclear translocation of proteins via the nuclear pore complex is dependent on a nuclear localization signal in the protein, which is rich in basic amino acids and may be bipartite [13][14][15]. The functional assays of such nuclear localization signals are usually based on the ability of a signal to confer nuclear localization to an otherwise non-nuclear protein.The present paper describes the occurrence of a novel TG that is localized exclusively in the nucleus of starfish (Asterina pectinifera) embryonic cells and is designated nuclear TG (nTG). The amino-acid sequence derived from the cDNA sequence contains putative nuclear localization signals [15] in the N-terminal region. We demonstrate here that the N-terminal region promotes the nuclear accumulation of an otherwise cytoplasmic protein, namely pyruvate kinase (PK), in the A. pectinifera oocyte system. This finding suggests that nuclear localization sig...

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Section: Immunofluorescence Microscopymentioning

confidence: 99%

Section: R E S U L T S Molecular Cloning Of a Pectinifera Transglutamentioning

confidence: 99%

Molecular characterization of a novel nuclear transglutaminase that is expressed during starfish embryogenesis

Sugino¹,

Terakawa²,

Yamasaki³

et al. 2002

Eur J Biochem

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“…5). The amino acid sequence was analyzed from the 19 peaks obtained, as shown in the Table. Among the peptides characterized, the presumed active site region comprising the pentapeptide TyrGly-Gln-Cys-Trp, 18) which is conserved in TGases, 19,20) The amino-terminal Ala residue of guinea pig liver TGase is numbered as 1.4) Asterisks indicate the identical amino acid residues.…”

Section: Partial Amino Acid Sequencingmentioning

confidence: 99%

Purification and Characterization of a Tissue-type Transglutaminase from Red Sea Bream (Pagrus major)

Yasueda

Kumazawa

Motoki

1994

Bioscience, Biotechnology, and Biochemistry

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“…We find that this transfer band is also present in mixtures of the mant nucleotides with the chicken red cell or the guinea pig liver TG, and it is interesting that, under identical conditions, the intensity of the 290-nm transfer band is twice as high with the chicken TG than with the human protein. Clearly, the Trp residues at conserved positions in these proteins (38) should be the best targets of point mutations for examining the question as to which contributes to the process of energy transfer to the nucleotide binding pocket of TG͞G h . Proximity and͞or the alignment between the relevant Trp residues and the mant group might be more favorable for energy transfer in chicken TG than in the human protein.…”

Section: Resultsmentioning

confidence: 99%

Nucleotide binding by the erythrocyte transglutaminase/G _h protein, probed with fluorescent analogs of GTP and GDP

Murthy

Lóránd²

2000

Proc. Natl. Acad. Sci. U.S.A.

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GTP is known to be a potent inhibitor of the protein crosslinking activity of transglutaminase (TG), probably the most abundant G protein in the human red cell. Nucleotide binding to TG was examined by fluorescence spectroscopy and anisotropy in mixtures of TG with methylanthraniloyl analogs of GTP and GDP. A characteristic feature was the appearance of a major energy transfer band ( exc, max ‫؍‬ 290 nm, em ‫؍‬ 444 nm) from protein tryptophans to the bound nucleotides. Quenching of the bound fluorophore ( exc ‫؍‬ 360 nm, em ‫؍‬ 444 nm) by acrylamide was barely different from that of free ligand. However, major changes were observed in anisotropy, which was used to demonstrate a facile exchange between bound and free nucleotides and to evaluate affinity constants for the binding of methylanthraniloyl GTP and GDP to TG.

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Cloning and expression of chicken erythrocyte transglutaminase.

Abstract: We

Cited by 32 publications

References 44 publications

Molecular characterization of a novel nuclear transglutaminase that is expressed during starfish embryogenesis

Molecular characterization of a novel nuclear transglutaminase that is expressed during starfish embryogenesis

Purification and Characterization of a Tissue-type Transglutaminase from Red Sea Bream (Pagrus major)

Nucleotide binding by the erythrocyte transglutaminase/G _h protein, probed with fluorescent analogs of GTP and GDP

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Cloning and expression of chicken erythrocyte transglutaminase.

Abstract: We

Cited by 32 publications

References 44 publications

Molecular characterization of a novel nuclear transglutaminase that is expressed during starfish embryogenesis

Molecular characterization of a novel nuclear transglutaminase that is expressed during starfish embryogenesis

Purification and Characterization of a Tissue-type Transglutaminase from Red Sea Bream (Pagrus major)

Nucleotide binding by the erythrocyte transglutaminase/G h protein, probed with fluorescent analogs of GTP and GDP

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Nucleotide binding by the erythrocyte transglutaminase/G _h protein, probed with fluorescent analogs of GTP and GDP