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FF Domains of CA150 Bind Transcription and Splicing Factors through Multiple Weak Interactions

机译：CA150的FF域通过多个弱相互作用绑定转录和剪接因子。

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摘要

The human transcription factor CA150 modulates human immunodeficiency virus type 1 gene transcription and contains numerous signaling elements, including six FF domains. Repeated FF domains are present in several transcription and splicing factors and can recognize phosphoserine motifs in the C-terminal domain (CTD) of RNA polymerase II (RNAPII). Using mass spectrometry, we identify a number of nuclear binding partners for the CA150 FF domains and demonstrate a direct interaction between CA150 and Tat-SF1, a protein involved in the coupling of splicing and transcription. CA150 FF domains recognize multiple sites within the Tat-SF1 protein conforming to the consensus motif (D/E)2/5-F/W/Y-(D/E)2/5. Individual FF domains are capable of interacting with Tat-SF1 peptide ligands in an equivalent and noncooperative manner, with affinities ranging from 150 to 500 μM. Repeated FF domains therefore appear to bind their targets through multiple weak interactions with motifs comprised of negatively charged residues flanking aromatic amino acids. The RNAPII CTD represents a consensus FF domain-binding site, contingent on generation of the requisite negative charges by phosphorylation of serines 2 and 5. We propose that CA150, through the dual recognition of acidic motifs in proteins such as Tat-SF1 and the phosphorylated CTD, could mediate the recruitment of transcription and splicing factors to actively transcribing RNAPII.
机译：人转录因子CA150调节人免疫缺陷病毒1型基因转录，并​​包含许多信号元件，包括六个FF域。重复的FF域存在于几个转录和剪接因子中，并且可以识别RNA聚合酶II（RNAPII）的C末端域（CTD）中的磷酸丝氨酸基序。使用质谱法，我们确定了CA150 FF域的许多核结合伴侣，并证明了CA150与Tat-SF1（参与剪接和转录偶联的蛋白质）之间的直接相互作用。 CA150 FF域识别Tat-SF1蛋白中符合一致基序（D / E） 2/5 -F / W / Y-（D / E） 2/5的多个位点。单个FF域能够以等效且非合作的方式与Tat-SF1肽配体相互作用，亲和力范围为150至500μM。因此，重复的FF结构域似乎通过与由芳香族氨基酸侧翼的带负电荷残基组成的基序的多次弱相互作用而结合其靶标。 RNAPII CTD代表一个共有的FF域结合位点，视丝氨酸2和5的磷酸化产生必需的负电荷而定。我们建议CA150通过双重识别蛋白质（如Tat-SF1和磷酸化的）中的酸性基序CTD可以介导转录和剪接因子的募集，以主动转录RNAPII。

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