THE LEISHMANIA-INFANTUM HISTONE H3 POSSESSES AN EXTREMELY DIVERGENT N-TERMINAL DOMAIN

被引：34

作者：

SOTO, M ^{[1
]}

REQUENA, JM ^{[1
]}

MORALES, G ^{[1
]}

ALONSO, C ^{[1
]}

机构：

[1] UNIV AUTONOMA MADRID,FAC CIENCIAS,CSIC,CTR BIOL MOLEC SEVERO OCHOA,E-28049 MADRID,SPAIN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1994年 / 1219卷 / 02期

关键词：

HISTONE H3; CDNA ISOLATION; ANTIGEN; (TRYPANOSOMATID);

D O I：

10.1016/0167-4781(94)90082-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The isolation of a Leishmania cDNA clone coding for an antigen identified as the histone H3 is described. The nucleotide sequence of the cDNA predicts that the Leishmania histone H3 contains 129 residues and that it has a molecular mass of 14620 Da. Comparison of the amino acid sequence with the consensus sequence of the eukaryotic histone H3 shows that the Leishmania protein has a highly conserved globular region and an extremely divergent amino-terminal portion.

引用

页码：533 / 535

页数：3

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