Biofilm formation by Bacillus subtilis requires an endoribonuclease-containing multisubunit complex that controls mRNA levels for the matrix gene repressor SinR.
Biofilm formation by Bacillus subtilis requires an endoribonuclease-containing multisubunit complex that controls mRNA levels for the matrix gene repressor SinR.
复制标题
DOI：
10.1111/mmi.13240
复制
发表时间：
2016-01
影响因子：
3.6
通讯作者：
Losick R
中科院分区：
文献类型：
--
作者：
DeLoughery A;Dengler V;Chai Y;Losick R
枯草芽孢杆菌生物膜的形成在很大程度上是由一个回路控制的，在这个回路中，反应调节器Spo0A打开了抗阻遏基因SINI的基因。反过来，SINI与SINR结合并使其失活，SINR是一种专门抑制基质产生的基因。基因ylbF、ymca和yaaT的突变在生物膜的形成中被阻止，但它们的作用机制一直是个谜。最近的一份报告将它们在生物膜形成中的作用归因于刺激Spo0A的活性。然而，我们没有发现对SINI转录的可测量的影响。相反，我们发现生物膜形成中的阻碍是由SinR及其mRNA水平的增加引起的。有证据表明，YlbF、YMCA和YaaT与RNaseY相互作用并控制RNaseY的活性，RNaseY是已知的破坏sinR mRNA稳定的RNaseY。我们发现RNaseY的另一个靶标cggR-GAPA mRNA的处理类似地依赖于YlbF和YMCA。我们的工作表明，sinR mRNA的稳定性是一种额外的转录后控制机制，控制着向多细胞的切换，并提出了YlbF、YMCA和YaaT作为含有RNaseY的多亚单位复合体的一部分来广泛调控mRNA稳定性的可能性。
Biofilm formation by Bacillus subtilis is largely governed by a circuit in which the response regulator Spo0A turns on the gene for the anti-repressor SinI. SinI, in turn, binds to and inactivates SinR, a dedicated repressor of genes for matrix production. Mutants of the genes ylbF, ymcA, and yaaT are blocked in biofilm formation, but the mechanism by which they act has been mysterious. A recent report attributed their role in biofilm formation to stimulating Spo0A activity. However, we detect no measurable effect on the transcription of sinI. Instead, we find that the block in biofilm formation is caused by an increase in the levels of SinR and of its mRNA. Evidence is presented that YlbF, YmcA and YaaT interact with, and control the activity of, RNase Y, which is known to destabilize sinR mRNA. We show that the processing of another target of RNase Y, cggR-gapA mRNA, similarly depends on YlbF and YmcA. Our work suggests that sinR mRNA stability is an additional posttranscriptional control mechanism governing the switch to multicellularity and raises the possibility that YlbF, YmcA, and YaaT broadly regulate mRNA stability as part of an RNase Y-containing, multi-subunit complex.