Brookman J L, Stott A J, Cheeseman P J, Adamson C S, Holmes D, Cole J, Burns N R
School of Biological Sciences, University of Manchester, United Kingdom.
Virology. 1995 Sep 10;212(1):69-76. doi: 10.1006/viro.1995.1454.
The yeast retrotransposon, Ty1, produces a macromolecular structure known as a virus-like particle (VLP) as an essential part of its replication cycle. The Ty1 Gag-like structural protein TYA, p1-440, alone is capable of directing assembly of the VLP. In order to determine the TYA sequences required for assembly, we have produced a series of truncated and deleted TYA forms and assessed their ability to assemble into particles. Removal of 100 amino acids from the C-terminus renders the TYA protein, p1-340, incapable of particle assembly; however, p1-363 with 77 residues missing from the C-terminus is capable of assembly. Removal of 40 amino acids from the N-terminus (p41-440 and p41-381) does not affect particle formation but more severely N-truncated forms, p71-381 and p100-381, are present as large aggregates within the cells and are therefore either incapable of or unavailable for VLP formation. Analysis of an internally deleted TYA, p1-381 delta 62-114, has identified this as a possible region of the TYA protein important for subunit:subunit interactions during the particle assembly.
酵母逆转录转座子Ty1在其复制周期的一个重要环节会产生一种被称为病毒样颗粒（VLP）的大分子结构。仅酵母Ty1类Gag结构蛋白TYA（p1 - 440）就能指导VLP的组装。为了确定组装所需的TYA序列，我们构建了一系列截短和缺失的TYA形式，并评估它们组装成颗粒的能力。从C末端去除100个氨基酸会使TYA蛋白p1 - 340无法组装成颗粒；然而，C末端缺失77个残基的p1 - 363却能够组装。从N末端去除40个氨基酸（p41 - 440和p41 - 381）并不影响颗粒形成，但N端截短程度更大的形式，如p71 - 381和p100 - 381，在细胞内以大聚集体形式存在，因此要么无法形成VLP，要么不能用于VLP形成。对内部缺失的TYA（p1 - 381 delta 62 - 114）的分析表明，这可能是TYA蛋白在颗粒组装过程中对亚基 - 亚基相互作用很重要的一个区域。
