Sequence-specific 1H, 13C and 15N signal assignments and secondary structure of archaeoglobusfulgidus SRP19.
Sequence-specific 1H, 13C and 15N signal assignments and secondary structure of archaeoglobusfulgidus SRP19.
复制标题
古生球菌 SRP19 的序列特异性 1H、13C 和 15N 信号分配和二级结构。
DOI：
10.1023/a:1011243402698
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发表时间：
2001
影响因子：
2.7
通讯作者：
Hinck,AP
中科院分区：
文献类型：
--
作者：
Pakhomova,ON;Cui,Y;Zwieb,C;Hinck,AP
The signal recognition particle (SRP) is an essential cytoplasmic ribonucleoprotein complex that is involved in targeting of signal-peptide-containing proteins to membranes. The 54 kDa protein component of the SRP, or SRP54, recognizes the signal peptides, interacts with a receptor on the membrane surface, and also binds to SRP RNA. Another SRP structural component, SRP19, which is the focus of this study, is the primary assembly protein of the mammalian SRP and obligatory for binding of SRP54 to the SRP RNA (Römisch et al., 1990). Eukaryotic polypeptides related to SRP19 have been identified in the genomes of Archaea, and recently the SRP of Archaeoglobus fulgidus has been sucessfully reconstituted from recombinant components (Bhuiyan et al., 2000). Site directed mutagenesis indicates that SRP19 has two binding sites in SRP RNA: a conserved tetraloop at the apex of helix 6, and three base pairs in the distal part of helix 8 (Zwieb, 1992, 1994). Both the N-and C-terminal regions of SRP19 are required for RNA binding (Chittenden et al., 1994). Since there is no evidence for interactions between SRP54 and SRP19 in the absence of RNA, binding of SRP19 to SRP RNA is believed to be accompanied by a conformational change in SRP RNA (Römisch et al., 1990). This model is supported by recent work which has shown that SRP19 induces conformational changes at an asymmetric bulge of helix 8 of SRP RNA located
