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Nuclear myosin II regulates the assembly of preinitiation complex for ICAM-1 gene transcription.

ABSTRACT: Actin-myosin II motor converts chemical energy into force/motion in muscle and nonmuscle cells. The phosphorylation of 20-kilodalton regulatory myosin light chain (MLC(20)) is critical to the cytoplasmic functions of these motors. We do not know whether myosin II and actins in the nucleus function as motors to generate relative motion, such as that between RNA polymerase II holoenzyme and DNA, for assembly of the preinitiation complex.The experiments were performed on primary cultures of human colonic circular smooth muscle cells and rat colonic circular muscle strips.We show that myosin II and alpha- and beta-actins are present in the nuclei of colonic smooth muscle cells. The nuclear myosin II is tethered to recognition sequence AGCTCC (-39/-34) in the intercellular adhesion molecule 1 (ICAM-1) core promoter region. The actins are known to complex with RNA polymerase II, and they are tethered to the nucleoskeleton. The dephosphorylation of MLC(20) increases the transcription of ICAM-1, whereas its phosphorylation decreases it. Colonic inflammation suppresses nuclear myosin light chain kinase, which increases the unphosphorylated form of nuclear MLC(20), resulting in enhanced transcription of ICAM-1.Myosin II is a core transcription factor. The phosphorylation/dephosphorylation of nuclear MLC(20) results in the sliding of myosin and actin molecules past each other, producing relative motion between DNA bound to the myosin II and RNA polymerase II holoenzyme bound to actins and nucleoskeleton.

SUBMITTER: Li Q

PROVIDER: S-EPMC2736361 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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Nuclear myosin II regulates the assembly of preinitiation complex for ICAM-1 gene transcription.

Li Qingjie Q Sarna Sushil K SK

Gastroenterology 20090326 3

<h4>Background & aims</h4>Actin-myosin II motor converts chemical energy into force/motion in muscle and nonmuscle cells. The phosphorylation of 20-kilodalton regulatory myosin light chain (MLC(20)) is critical to the cytoplasmic functions of these motors. We do not know whether myosin II and actins in the nucleus function as motors to generate relative motion, such as that between RNA polymerase II holoenzyme and DNA, for assembly of the preinitiation complex.<h4>Methods</h4>The experiments wer ...[more]

PMID: 19328794

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Project description:During their productive cycle, herpesviruses exhibit a strictly regulated temporal cascade of gene expression that has three general stages: immediate early (IE), early (E), and late (L). Promoter complexity differs strikingly between IE/E genes and L genes. IE and E promoters contain cis-regulating sequences upstream of a TATA box, whereas L promoters comprise a unique cis element. In the case of the gammaherpesviruses, this element is usually a TATT motif found in the position where the consensus TATA box of eukaryotic promoters is typically found. Epstein-Barr virus (EBV) encodes a protein, called BcRF1, which has structural homology with the TATA-binding protein and interacts specifically with the TATT box. However, although necessary for the expression of the L genes, BcRF1 is not sufficient, suggesting that other viral proteins are also required. Here, we present the identification and characterization of a viral protein complex necessary and sufficient for the expression of the late viral genes. This viral complex is composed of five different proteins in addition to BcRF1 and interacts with cellular RNA polymerase II. During the viral productive cycle, this complex, which we call the vPIC (for viral preinitiation complex), works in concert with the viral DNA replication machinery to activate expression of the late viral genes. The EBV vPIC components have homologs in beta- and gammaherpesviruses but not in alphaherpesviruses. Our results not only reveal that beta- and gammaherpesviruses encode their own transcription preinitiation complex responsible for the expression of the late viral genes but also indicate the close evolutionary history of these viruses.Control of late gene transcription in DNA viruses is a major unsolved question in virology. In eukaryotes, the first step in transcriptional activation is the formation of a permissive chromatin, which allows assembly of the preinitiation complex (PIC) at the core promoter. Fixation of the TATA box-binding protein (TBP) is a key rate-limiting step in this process. This study provides evidence that EBV encodes a complex composed of six proteins necessary for the expression of the late viral genes. This complex is formed around a viral TBP-like protein and interacts with cellular RNA polymerase II, suggesting that it is directly involved in the assembly of a virus-specific PIC (vPIC).

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Nuclear myosin II regulates the assembly of preinitiation complex for ICAM-1 gene transcription.

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Nuclear myosin II regulates the assembly of preinitiation complex for ICAM-1 gene transcription.

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