LSm proteins form heptameric rings that bind to RNA via repeating motifs

被引:91
作者
Khusial, P [1 ]
Plaag, R [1 ]
Zieve, GW [1 ]
机构
[1] SUNY Stony Brook, Dept Pathol, Stony Brook, NY 11794 USA
关键词
D O I
10.1016/j.tibs.2005.07.006
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
Members of the LSm family of proteins share the Sm fold - a closed barrel comprising five anti-parallel beta strands with an alpha helix stacked on the top. The fold forms a subunit of hexameric or heptameric rings of similar to 7 nm in diameter. Interactions between neighboring subunits center on an anti-parallel interaction of the fourth and fifth beta strands. In the lumen of the ring, the subunits have the same spacing as nucleotides in RNA, enabling the rings to bind to single-stranded RNA via a repeating motif. Eubacteria and archaea build homohexamers and homoheptamers, respectively, whereas eukaryotes use > 18 LSm paralogs to build at least six different heteroheptameric rings. The four different rings in the nucleus that permanently bind small nuclear RNAs and function in pre-mRNA maturation are called Sm rings. The two different rings that transiently bind to RNAs and, thereby, assist in the degradation of mRNA in the cytoplasm and the maturation of a wide spectrum of RNAs in the nucleus are called LSm rings.
引用
收藏
页码:522 / 528
页数:7
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