-transparent.png){kind=logo}
We have evidence that the limulus (Tachypleus tri-dentatus) hemocyte transglutaminase (TGase) has a molecular mass of 86 kDa and properties of the mammalian type II TGase-like enzyme (Tokunaga, F., Yamada, M., Miyata, T., Ding, Y.-L., Hiranaga-Kawabata, M., Muta, T., Iwanaga, S., Ichinose, A., and Davie, E.W. (1993) J. Biol. Chem. 268, 252-261). We present here the cDNA and amino acid sequences, and localization of the TGase in various tissues of limulus. The cloned cDNA for TGase consists of 2,884 base pairs. An open reading frame of 2,292 base pairs encodes a sequence comprising 764 residues of the mature protein with molecular masses of 87,021 and 87,110 Da, due to two different clones. The discrepancies of nucleotides in these two clones result in 3 amino acid exchanges at positions Gly452(GGT)-Arg(CGT), Ser477(AGT)-Cys(TGT), and Ile486(ATC)-Ser(AGC), respectively. Northern blot analysis on a total RNA extracted from various tissues of limulus revealed that TGase is expressed with 3.0 kilobases of a single type of mRNA, mainly in hemocytes, hepatopancreas, and gastric tissues. Limulus TGase shows significant sequence similarity with the mammalian TGase family, as follows: guinea pig liver TGase (32.7%), human factor XIIIa subunit (34.7%), human keratinocyte TGase (37.6%), and human erythrocyte band 4.2 (23.0%). Limulus TGase has a unique NH2-terminal cationic extension of 60 residues with no homology to the NH2 termini of mammalian TGases. Based on the alignment of the amino acid sequence of limulus TGase with those of the known TGase family, a phylogenetic tree representing an evolutionary relationship among the family members was inferred by the neighbor joining method.
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
September 1996,
The Journal of biological chemistry,
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
April 1988,
Biochemistry,
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
January 1995,
The Journal of biological chemistry,
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
September 1989,
Biochemical and biophysical research communications,
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
April 1983,
Biochemical and biophysical research communications,
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
June 1988,
The Journal of biological chemistry,
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
October 1989,
Biochemistry,
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
May 2001,
Journal of protein chemistry,
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
May 2007,
Fish & shellfish immunology,
F Tokunaga, and
T Muta, and
S Iwanaga, and
A Ichinose, and
E W Davie, and
K Kuma, and
T Miyata
November 1996,
Bioscience, biotechnology, and biochemistry,
