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人 La 相关蛋白 1 的 La 基序的 H、C 和 N 共振分配。

H, C, and N resonance assignments of the La Motif of the human La-related protein 1.

机构信息

Department of Chemistry & Biochemistry, Florida State University, Tallahassee, FL, 32306, USA.

Institute of Molecular Biophysics, Florida State University, Tallahassee, FL, 32306, USA.

出版信息

Biomol NMR Assign. 2024 Jun;18(1):111-118. doi: 10.1007/s12104-024-10176-4. Epub 2024 May 1.

Abstract

Human La-related protein 1 (HsLARP1) is involved in post-transcriptional regulation of certain 5' terminal oligopyrimidine (5'TOP) mRNAs as well as other mRNAs and binds to both the 5'TOP motif and the 3'-poly(A) tail of certain mRNAs. HsLARP1 is heavily involved in cell proliferation, cell cycle defects, and cancer, where HsLARP1 is significantly upregulated in malignant cells and tissues. Like all LARPs, HsLARP1 contains a folded RNA binding domain, the La motif (LaM). Our current understanding of post-transcriptional regulation that emanates from the intricate molecular framework of HsLARP1 is currently limited to small snapshots, obfuscating our understanding of the full picture on HsLARP1 functionality in post-transcriptional events. Here, we present the nearly complete resonance assignment of the LaM of HsLARP1, providing a significant platform for future NMR spectroscopic studies.

摘要

人类 La 相关蛋白 1(HsLARP1)参与某些 5'端寡嘧啶(5'TOP)mRNA 以及其他 mRNA 的转录后调控,与某些 mRNA 的 5'TOP 基序和 3'-多聚(A)尾结合。HsLARP1 大量参与细胞增殖、细胞周期缺陷和癌症,恶性细胞和组织中 HsLARP1 显著上调。与所有 LARPs 一样,HsLARP1 含有一个折叠的 RNA 结合域,即 La 基序(LaM)。目前我们对 HsLARP1 复杂分子结构所产生的转录后调控的理解仅限于一些小的快照,这阻碍了我们对 HsLARP1 在转录后事件中的功能的全面理解。在这里,我们呈现了 HsLARP1 的 LaM 的几乎完整的共振分配,为未来的 NMR 光谱研究提供了一个重要的平台。

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