SPLICE SITE SELECTION IN THE PROTEOLIPID PROTEIN (PLP) GENE TRANSCRIPT AND PRIMARY STRUCTURE OF THE DM-20 PROTEIN OF CENTRAL-NERVOUS-SYSTEM MYELIN
SPLICE SITE SELECTION IN THE PROTEOLIPID PROTEIN (PLP) GENE TRANSCRIPT AND PRIMARY STRUCTURE OF THE DM-20 PROTEIN OF CENTRAL-NERVOUS-SYSTEM MYELIN
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DOI：
10.1073/pnas.84.16.5665
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发表时间：
1987-08-01
影响因子：
11.1
通讯作者：
MILNER, RJ
中科院分区：
文献类型：
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作者：
NAVE, KA;LAI, C;MILNER, RJ
蛋白脂质蛋白（PLP）是中枢神经系统的主要髓磷脂膜蛋白。我们从小鼠大脑 cDNA 文库中分离出一份选择性剪接的 PLP 基因转录本，并筛选了 PLP 相关序列。所编码的 241 个氨基酸蛋白与 PLP 的不同之处在于从主要亲水结构域内部删除了 35 个氨基酸残基 (116-150)。这种 PLP 变体与髓鞘质的 DM-20 蛋白相同，后者先前被描述为大脑特异性髓鞘质成分，并且已知与 PLP 相关。我们确定了大鼠 PLP 基因的相应核苷酸序列，发现当位于初级 PLP 转录本第三外显子内 105 个核苷酸的第二个 5'' 剪接位点用于前体 mRNA (pre-mRNA) 剪接时，就会产生 DM-20 mRNA。这表明选择性5''剪接位点选择可以确定细胞基因的蛋白质产物。 DM-20 mRNA 在大鼠脑中表达，相对于 PLP mRNA 丰度约为 50%，并且似乎在发育过程中受到共同调节。
Proteolipid protein (PLP) is the major myelin membrane protein of the central nervous system. We have isolated a copy of an alternatively spliced PLP gene transcript from a mouse brain cDNA library that was screened for PLP-related sequences. The encoded 241-amino acid protein differs from PLP by an internal deletion of 35-amino acid residues (116-150) from the major hydrophilic domain. This PLP variant is identical with the DM-20 protein of myelin, previously described as a brain-specific myelin component and known to be related to PLP. We determined the corresponding nucleotide sequence of the rat PLP gene and found that DM-20 mRNA results when a second 5'' splice site, located 105 nucleotides within the third exon of the primary PLP transcript, is utilized in precursor mRNA (pre-mRNA) splicing. This demonstrates that alternative 5'' splice site selection can determine the protein product of a cellular gene. DM-20 mRNA is expressed in rat brain with approximately 50% abundance relative to PLP mRNA and appears to be developmentally coregulated.