Limulus hemocyte transglutaminase. cDNA cloning, amino acid sequence, and tissue localization.
Limulus hemocyte transglutaminase. cDNA cloning, amino acid sequence, and tissue localization.
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DOI：
10.1016/s0021-9258(18)54144-2
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发表时间：
1993-01
期刊：
影响因子：
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通讯作者：
F. Tokunaga;T. Muta;S. Iwanaga;A. Ichinose;E. Davie;K. Kuma;Toshio Miyata
中科院分区：
文献类型：
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作者：
F. Tokunaga;T. Muta;S. Iwanaga;A. Ichinose;E. Davie;K. Kuma;Toshio Miyata
我们有证据表明，河蟹(Tachypleus tri-Dentatus)血细胞转谷氨酰胺酶(TGase)的分子质量为86 kDa，并具有哺乳动物II型TGase的性质(Tokunaga，F.，Yamada，M.，Miyata，T.，Ding，Y.-L.，Hiranaga-Kawabata，M.，Muta，T.，Iwanaga，S.，Ichinose，A.，和Davie，E.W.(1993)J.Biol)。化学。268、252-261)。本文介绍了TGase的基因序列和氨基酸序列，以及TGase在不同组织中的定位。克隆的TGase基因全长2,884个碱基。2,292个碱基对的开放阅读框编码了一个由764个残基组成的成熟蛋白序列，分子质量分别为87,021和87,110 Da，这是由于两个不同的克隆所致。这两个克隆中核苷酸的差异导致了3个氨基酸交换，分别位于Gly452(GGT)-Arg(CGT)、Ser477(AGT)-Cys(TGT)和Ile486(ATC)-Ser(AGC)。Northern杂交分析表明，TGase主要在血细胞、肝胰腺和胃组织中表达，其大小约为3.0kb。TGase与哺乳动物TGase家族有显著的序列相似性，分别为：豚鼠肝脏TGase(32.7%)、人凝血因子XIIIA亚单位(34.7%)、人角质形成细胞TGase(37.6%)和人红细胞条带4.2(23.0%)。该酶具有独特的60个残基的氨基末端阳离子延伸，与哺乳动物TGase的氨基末端没有同源性。通过与已知TGase家族氨基酸序列的比对，用邻接法构建了代表家族成员间进化关系的系统发育树。
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.