NUCLEOTIDE-SEQUENCE OF A COMPLETE MOUSE INTRACISTERNAL-A-PARTICLE GENOME - RELATIONSHIP TO KNOWN ASPECTS OF PARTICLE ASSEMBLY AND FUNCTION
NUCLEOTIDE-SEQUENCE OF A COMPLETE MOUSE INTRACISTERNAL-A-PARTICLE GENOME - RELATIONSHIP TO KNOWN ASPECTS OF PARTICLE ASSEMBLY AND FUNCTION
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DOI：
10.1128/jvi.61.10.3020-3029.1987
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发表时间：
1987-10-01
影响因子：
5.4
通讯作者：
KUFF, EL
中科院分区：
文献类型：
--
作者：
MIETZ, JA;GROSSMAN, Z;KUFF, EL
本文报道了小鼠脑池内A颗粒（IAP）元件MIA 14的7，095个核苷酸的序列。已知MIA 14与IAP 35 S RNA共线性，并含有功能性长末端重复序列。它的内部遗传组织是通过与同源的叙利亚仓鼠元件和相关的逆转录病毒猿逆转录病毒1（猿D型）和劳斯肉瘤病毒（禽C型）的比较确定的。MIA 14含有827个密码子的gag-蛋白酶开放阅读框和通过-1移码进入的867个密码子的pol区。1，100个碱基对的env区域在所有阅读框中具有多个终止密码子，这与迄今为止未能检测到IAP相关糖基化包膜组分一致。在体外从含有紧密同源的gag-蛋白酶开放阅读框的cDNA克隆转录的RNA在无细胞系统中翻译。主要产物是一种73千道尔顿的多肽，可与抗真正的IAP gag相关结构蛋白p73的抗血清免疫沉淀。而不是结束在gag蛋白酶的边界，p73似乎含有7至8千道尔顿的肽编码的蛋白酶结构域，一个特异性可能与观察到的损害正常蛋白质加工的IAP。gag的N-末端217个密码子是鼠IAP所特有的，并且可能是通过与细胞基因重组而贡献的。gag的小鼠特异性区域编码具有非典型切割位点的疏水信号肽。该肽的延迟切割可能导致新合成的p73锚定到内质网膜上，并限制颗粒组装到该位点。
The 7,095-nucleotide sequence of a mouse genomic intracisternal A-particle (IAP) element, MIA14, is reported. MIA14 is known to be colinear with IAP 35S RNA and to contain functional long terminal repeats. Its internal genetic organization was determined by comparisons with a homologous Syrian hamster element and the related retroviruses simian retrovirus 1 (simian type D) and Rous sarcoma virus (avian type C). MIA14 contains a gag-protease open reading frame of 827 codons and a pol region of 867 codons entered by a frame shift of -1. The env region of 1,100 base pairs has multiple stop codons in all reading frames, consistent with the failure thus far to detect IAP-related glycosylated envelope components. RNA transcribed in vitro from a cDNA clone containing a closely homologous gag-protease open reading frame was translated in a cell-free system. The main product was a 73-kilodalton polypeptide immunoprecipitable with antiserum against the authentic IAP gag-related structural protein p73. Rather than ending at the gag-protease boundary, p73 appears to contain 7 to 8 kilodaltons of peptide encoded by the protease domain, a peculiarity possibly related to the observed impairment of normal protein processing in IAPs. The N-terminal 217 codons of gag are unique to murine IAPs and may have been contributed by recombination with a cellular gene. The mouse-specific region of gag encodes a hydrophobic signal peptide with an atypical cleavage site. Delayed cleavage of this peptide could result in anchoring of newly synthesized p73 to the endoplasmic reticulum membrane and restriction of particle assembly to this site.