May G S, Morris N R
Department of Pharmacology, UMDNJ, Robert Wood Johnson Medical School, Piscataway 08854.
Gene. 1987;58(1):59-66. doi: 10.1016/0378-1119(87)90029-1.
The histone H2A gene of the filamentous fungus Aspergillus nidulans has been cloned and sequenced. There is a single H2A gene in the genome of A. nidulans, and it contains three introns. The introns are 51 nucleotides (nt), 56 nt and 50 nt in length and split codons for amino acids (aa) 18, 48 and 116 of the predicted protein. The transcriptional start and termination points have been determined using an S1 nuclease protection assay. The predicted protein is 132 aa residues in length and surprisingly has a threonine after the initiator methionine instead of the usual serine. The sequence of the predicted histone H2A protein is compared to histone H2A proteins from Schizosaccharomyces pombe, Saccharomyces cerevisiae and calf thymus. Comparison of the amino acid sequence to these other H2A proteins shows that the divergence of amino acid sequences between H2A proteins is found in two clustered sites.
丝状真菌构巢曲霉的组蛋白H2A基因已被克隆和测序。构巢曲霉基因组中只有一个H2A基因，它含有三个内含子。这些内含子长度分别为51个核苷酸（nt）、56 nt和50 nt，将预测蛋白质中第18、48和116位氨基酸（aa）的密码子隔开。转录起始点和终止点已通过S1核酸酶保护试验确定。预测的蛋白质长度为132个氨基酸残基，令人惊讶的是，起始甲硫氨酸之后是苏氨酸，而不是通常的丝氨酸。将预测的组蛋白H2A蛋白质序列与来自粟酒裂殖酵母、酿酒酵母和小牛胸腺的组蛋白H2A蛋白质进行比较。将氨基酸序列与这些其他H2A蛋白质进行比较表明，H2A蛋白质之间氨基酸序列的差异存在于两个聚集位点。
