Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.7.6 (RNA polymerase)
34,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Actin and myosin have been individually implicated in different aspects of gene expression. Here, we show in vivo evidence for a specific nucleolar actin-myosin complex physically associated with both the RNA polymerase I holoenzyme and ribosomal genes. We find that this specific actin-myosin complex is functionally coupled to elongating ribosomal RNA transcripts in living cells. From these observations, we conclude that an actin-based myosin motor is associated with transcribing ribosomal genes in the cell nucleus. These results correlate with an involvement of both actin and myosin in regulating mRNA synthesis and suggest that actin-myosin motors may provide a general mechanism to facilitate elongation of RNA transcripts during transcription of both ribosomal genes and protein-coding genes.
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PMID:An actin-myosin complex on actively transcribing genes. 1498 May 9

Biological and engineered motors are surprisingly similar in their adherence to two or possibly three fundamental regimes for the mass scaling of maximum force output (Fmax). One scaling regime (Group 1: myosin, kinesin, dynein and RNA polymerase molecules; muscle cells; whole muscles; winches; linear actuators) comprises motors that create slow translational motion with force outputs limited by the axial stress capacity of the motor, which results in Fmax scaling as motor mass0.67 (M0.67). Another scaling regime (Group 2: flying birds, bats and insects; swimming fish; running animals; piston engines; electric motors; jets) comprises motors that cycle rapidly, with significant internal and external accelerations, and for whom inertia and fatigue life appear to be important constraints. The scaling of inertial loads and fatigue life both appear to enforce Fmax scaling as M1.0 in these motors. Despite great differences in materials and mechanisms, the mass specific Fmax of Group 2 motors clusters tightly around a mean of 57 N kg(-1), a region of specific force loading where there appears to be a common transition from high- to low-cycle fatigue. For motors subject to multi-axial stresses, the steepness of the load-life curve in the neighborhood of 50-100 N kg(-1) may overwhelm other material and mechanistic factors, thereby homogenizing the mass specific Fmax of grossly dissimilar animals and machines. Rockets scale with Group 1 motors but for different mechanistic reasons; they are free from fatigue constraints and their thrust is determined by mass flow rates that depend on cross sectional area of the exit nozzle. There is possibly a third scaling regime of Fmax for small motors (bacterial and spermatazoan flagella; a protozoan spring) where viscosity dominates over inertia. Data for force output of viscous regime motors are scarce, but the few data available suggest a gradually increasing scaling slope that converges with the Group 2 scaling relationship at a Reynolds number of about 10(2). The Group 1 and Group 2 scaling relationships intersect at a motor mass of 4400 kg, which restricts the force output and design of Group 2 motors greater than this mass. Above 4400 kg, all motors are limited by stress and have Fmax that scales as M0.67; this results in a gradual decline in mass specific Fmax at motor mass greater than 4400 kg. Because of declining mass specific Fmax, there is little or no potential for biological or engineered motors or rockets larger than those already in use.
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PMID:Scaling of maximum net force output by motors used for locomotion. 1585 97

The proteins actin and myosin have a firm place in the muscles, where they are responsible for contraction. Although recent investigations have shown that they are found in the nucleus, it has been unclear as to what they are doing there. The discovery of actin as a component of the transcription apparatus, chromatin-remodeling complexes, as well as RNA processing machines, implies important roles for actin in the readout of genetic information. Actin is associated with all three nuclear RNA polymerases and acts in concert with nuclear myosin 1 (NM1) to drive transcription. Actin-NMI interactions are involved in the transition of the initiation complex into the elongation complex, presumably by triggering a structural change of the transcription apparatus or by generating force that supports RNA polymerase movement.
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PMID:Actin and myosin as transcription factors. 1649 46

Nuclear actin and myosin 1 (NM1) are key regulators of gene transcription. Here, we show by biochemical fractionation of nuclear extracts, protein-protein interaction studies and chromatin immunoprecipitation assays that NM1 is part of a multiprotein complex that contains WICH, a chromatin remodelling complex containing WSTF (Williams syndrome transcription factor) and SNF2h. NM1, WSTF and SNF2h were found to be associated with RNA polymerase I (Pol I) and ribosomal RNA genes (rDNA). RNA interference-mediated knockdown of NM1 and WSTF reduced pre-rRNA synthesis in vivo, and antibodies to WSTF inhibited Pol I transcription on pre-assembled chromatin templates but not on naked DNA. The results indicate that NM1 cooperates with WICH to facilitate transcription on chromatin.
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PMID:The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin 1 and has a role in RNA polymerase I transcription. 1651 17

Transcription in eukaryotic cells requires dynamic changes of chromatin structure to facilitate or prevent RNA polymerase access to active genes. These structural modifications rely on the concerted action of ATP-dependent chromatin-remodelling complexes and histone-modifying enzymes, which generate a chromatin configuration that is either compatible with transcription (euchromatin) or incompatible (heterochromatin). Insights into how these structural changes might be coordinated for RNA polymerase I (pol I) genes come from the discoveries of the nucleolar-remodelling complex (NoRC) and B-WICH--a high molecular weight fraction of the WSTF/SNF2h chromatin-remodelling complex. NoRC produces a repressive chromatin state; B-WICH, together with nuclear myosin 1, activates pol I transcription directly on chromatin templates and might also function in the maintenance of ribosomal chromatin structure.
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PMID:Chromatin remodelling and transcription: be-WICHed by nuclear myosin 1. 1657 91

The WSTF (Williams syndrome transcription factor) protein is involved in vitamin D-mediated transcription and replication as a component of two distinct ATP-dependent chromatin remodeling complexes, WINAC and WICH, respectively. We show here that the WICH complex (WSTF-SNF2h) interacts with several nuclear proteins as follows: Sf3b155/SAP155, RNA helicase II/Gualpha, Myb-binding protein 1a, CSB, the proto-oncogene Dek, and nuclear myosin 1 in a large 3-MDa assembly, B-WICH, during active transcription. B-WICH also contains RNAs, 45 S rRNA, 5 S rRNA, 7SL RNA, and traces of the U2 small nuclear RNA. The core proteins, WSTF, SNF2h, and nuclear myosin 1, are associated with the RNA polymerase III genes 5 S rRNA genes and 7SL, and post-transcriptional silencing of WSTF reduces the levels of these transcripts. Our results show that a WSTF-SNF2h assembly is involved in RNA polymerase III transcription, and we suggest that WSTF-SNF2h-NM1 forms a platform in transcription while providing chromatin remodeling.
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PMID:The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription. 1660 71

Molecular motors, such as kinesin, myosin, or dynein, convert chemical energy into mechanical energy by hydrolyzing ATP. The mechanical energy is used for moving in discrete steps along the cytoskeleton and carrying a molecular load. High resolution single molecule recordings of motor steps appear as a stochastic sequence of dwells, resembling a staircase. Staircase data can also be obtained from other molecular machines such as F1 -ATPase, RNA polymerase, or topoisomerase. We developed a maximum likelihood algorithm that estimates the rate constants between different conformational states of the protein, including motor steps. We model the motor with a periodic Markov model that reflects the repetitive chemistry of the motor step. We estimated the kinetics from the idealized dwell-sequence by numerical maximization of the likelihood function for discrete-time Markov models. This approach eliminates the need for missed event correction. The algorithm can fit kinetic models of arbitrary complexity, such as uniform or alternating step chemistry, reversible or irreversible kinetics, ATP concentration and mechanical force-dependent rates, etc. The method allows global fitting across stationary and nonstationary experimental conditions, and user-defined a priori constraints on rate constants. The algorithm was tested with simulated data, and implemented in the free QuB software.
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PMID:Maximum likelihood estimation of molecular motor kinetics from staircase dwell-time sequences. 1667 62

Processive molecular motors, such as kinesin, myosin, or dynein, convert chemical energy into mechanical energy by hydrolyzing ATP. The mechanical energy is used for moving in discrete steps along the cytoskeleton and carrying a molecular load. Single-molecule recordings of motor position along a substrate polymer appear as a stochastic staircase. Recordings of other single molecules, such as F1-ATPase, RNA polymerase, or topoisomerase, have the same appearance. We present a maximum likelihood algorithm that extracts the dwell time sequence from noisy data, and estimates state transition probabilities and the distribution of the motor step size. The algorithm can handle models with uniform or alternating step sizes, and reversible or irreversible kinetics. A periodic Markov model describes the repetitive chemistry of the motor, and a Kalman filter allows one to include models with variable step size and to correct for baseline drift. The data are optimized recursively and globally over single or multiple data sets, making the results objective over the full scale of the data. Local binary algorithms, such as the t-test, do not represent the behavior of the whole data set. Our method is model-based, and allows rapid testing of different models by comparing the likelihood scores. From data obtained with current technology, steps as small as 8 nm can be resolved and analyzed with our method. The kinetic consequences of the extracted dwell sequence can be further analyzed in detail. We show results from analyzing simulated and experimental kinesin and myosin motor data. The algorithm is implemented in the free QuB software.
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PMID:Extracting dwell time sequences from processive molecular motor data. 1690 7

Myosin VI is the only myosin that moves toward the minus end of actin filaments, suggesting a unique biological function. Here, we show that myosin VI is present in the nucleus of mammalian cells where it colocalizes with newly transcribed mRNA and with RNA polymerase II (RNAPII) and is detected in the RNAPII complex. The colocalization and interaction of myosin VI with RNAPII require transcriptional activity. Chromatin immunoprecipitation (ChIP) demonstrates that myosin VI is recruited to the promoter and intragenic regions of active genes, encoding urokinase plasminogen activator (uPA), eukaryotic initiation factor 6 (p27/eIF6), and low-density lipoprotein receptor (LDLR), but not to noncoding, nonregulatory intergenic regions. Downregulation of myosin VI reduces steady-state mRNA levels of these genes in vivo, and antibodies to myosin VI reduce transcription in vitro. We suggest that myosin VI modulates RNAPII-dependent transcription of active genes, implicating the possibility of an actin-myosin based mechanism of transcription.
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PMID:Nuclear myosin VI enhances RNA polymerase II-dependent transcription. 1694 70

The nuclear isoform of myosin, Nuclear Myosin I (NMI) is involved in transcription by RNA polymerase I. Previous experiments showing that antibodies to NMI inhibit transcription by RNA polymerase II using HeLa cell nuclear extract (NE) suggested that NMI might be a general transcription factor for RNA polymerases. In this study we used a minimal in vitro transcription system to investigate the involvement of NMI in transcription by RNA polymerase II in detail. We demonstrate that NMI co-purifies with RNA polymerase II and that NMI is necessary for basal transcription by RNA polymerase II because antibodies to NMI inhibit transcription while adding NMI stimulates transcription. Further investigation revealed that NMI is specifically involved in transcription initiation. Finally, by employing an abortive transcription initiation assay, we demonstrate that NMI is crucial for the formation of the first phosphodiester bond during transcription initiation.
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PMID:Nuclear myosin I is necessary for the formation of the first phosphodiester bond during transcription initiation by RNA polymerase II. 1696 Aug 72


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