The carboxyterminal zinc fingers of TFIIIA interact with the tip of helix V of 5S RNA in the 7S ribonucleoprotein particle.
The carboxyterminal zinc fingers of TFIIIA interact with the tip of helix V of 5S RNA in the 7S ribonucleoprotein particle.
复制标题
TFIIIA 的羧基末端锌指与 7S 核糖核蛋白颗粒中 5S RNA 的螺旋 V 尖端相互作用。
DOI：
10.1093/nar/19.8.1791
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发表时间：
1991
影响因子：
14.9
通讯作者：
Bogenhagen,DF
中科院分区：
文献类型：
--
作者：
Sands,MS;Bogenhagen,DF
ImmatureXenopus laevisoocytes contain large quantities of a 7S ribonucleoprotein particle containing transcription factor IIIA (IFIIIA) and 5S RNA in a 1:1 molar ratio. We have reconstituted RNPs containing 5S RNA and either intact TFIIIA or proteoiytic fragments that represent progressive C-terminal deletions of the protein. A partial trypsin digestion fragment encompassing the amino terminal seven zinc fingers of TFIIIA rebinds 5S RNA with nearly the same affinity as intact TFIIIA. We have compared the RNase protection patterns resulting from binding of intact and deleted forms of TFIIIA. RNAse protection assays using cobra venom nuclease were performed on complexes reconstituted with 5′ and 3′ end-labeled 5S RNA. Similar experiments with 3′ end-labeled 5S RNA were performed with nuclease α-sarcin. With both nucleases, nucleotides in helix V of 5S RNA show more complete protection from nuclease cleavage when the RNA is bound to intact TFIIIA than when it is bound to a 20 kDa tryptic fragment of TFIIIA lacking the C-terminal portion of the protein. These results suggest that fingers 8 and 9 of TF1IIA interact with the distal portion of helix V in the 5S RNA.
