| RfaH Counter-Silences Inhibition of Transcript Elongation by H-NS-StpA Nucleoprotein Filaments in Pathogenic Escherichia coli. | RfaH Counter-Silences Inhibition of Transcript Elongation by H-NS-StpA Nucleoprotein Filaments in Pathogenic Escherichia coli.
Hustmyer CM, Wolfe MB, Welch RA, Landick R., Free PMC Article | 03/2/2023 |
| The RNA chaperone StpA enables fast RNA refolding by destabilization of mutually exclusive base pairs within competing secondary structure elements. | The RNA chaperone StpA enables fast RNA refolding by destabilization of mutually exclusive base pairs within competing secondary structure elements.
Hohmann KF, Blümler A, Heckel A, Fürtig B., Free PMC Article | 12/25/2021 |
| StpA represses CRISPR-Cas immunity in H-NS deficient Escherichia coli. | StpA represses CRISPR-Cas immunity in H-NS deficient Escherichia coli.
Mitić D, Radovčić M, Markulin D, Ivančić-Baće I. | 01/16/2021 |
| Hha and StpA greatly enhance H-NS-stimulated pausing by RNAP at 20 degrees C. StpA:H-NS or StpA-only filaments also stimulate pausing at 37 degrees C, a temperature at which Hha:H-NS or H-NS-only filaments have much less effect. In addition, both Hha and StpA greatly stimulate DNA-DNA bridging by H-NS filaments. | StpA and Hha stimulate pausing by RNA polymerase by promoting DNA-DNA bridging of H-NS filaments.
Boudreau BA, Hron DR, Qin L, van der Valk RA, Kotlajich MV, Dame RT, Landick R., Free PMC Article | 07/27/2019 |
| three new candidates of E. coli nucleoid, namely DNA-binding protein from starved cells (Dps), host factor for phage Qbeta (Hfq) and suppressor of td(-) phenotype A (StpA) | Growth phase dependent changes in the structure and protein composition of nucleoid in Escherichia coli.
Talukder A, Ishihama A. | 07/30/2016 |
| Also, DeltahnsDeltastpA double mutants simultaneously lacking H-NS and its paralog StpA showed more severe reductions in ompW expression at 37 degrees C, resulting in the complete loss of OmpW. | Expression of the Escherichia coli ompW colicin S4 receptor gene is regulated by temperature and modulated by the H-NS and StpA nucleoid-associated proteins.
Brambilla L, Morán-Barrio J, Viale AM. | 11/22/2014 |
| Both the DNA binding sites of H-NS as well as the function of StpA as a backup system might be selected for silencing highly transcribable genes. | Genomic analysis reveals epistatic silencing of "expensive" genes in Escherichia coli K-12.
Srinivasan R, Chandraprakash D, Krishnamurthi R, Singh P, Scolari VF, Krishna S, Seshasayee AS. | 01/25/2014 |
| In contrast to H-NS, the StpA filament interacts with a naked DNA segment to cause DNA bridging which results in simultaneous stiffening and bridging of DNA. | Gene silencing H-NS paralogue StpA forms a rigid protein filament along DNA that blocks DNA accessibility.
Lim CJ, Whang YR, Kenney LJ, Yan J., Free PMC Article | 07/14/2012 |
| StpA binding profile reduced to one-third in the hns mutant and the H-NS binding profile was unaffected by stpA inactivation. | Differential binding profiles of StpA in wild-type and h-ns mutant cells: a comparative analysis of cooperative partners by chromatin immunoprecipitation-microarray analysis.
Uyar E, Kurokawa K, Yoshimura M, Ishikawa S, Ogasawara N, Oshima T., Free PMC Article | 01/21/2010 |
| StpA in homologous recombination and double-strand break repair is discussed | Roles of the DNA binding proteins H-NS and StpA in homologous recombination and repair of bleomycin-induced damage in Escherichia coli.
Shiraishi K, Ogata Y, Hanada K, Kano Y, Ikeda H. | 01/21/2010 |
| N-terminus verified by Edman degradation on mature peptide | Escherichia coli protein StpA stimulates self-splicing by promoting RNA assembly in vitro.
Zhang A, Derbyshire V, Salvo JL, Belfort M., Free PMC Article | 11/5/2007 |
| The structural stability of an RNA determines whether the RNA chaperone activity of StpA is beneficial to folding. | Influence of RNA structural stability on the RNA chaperone activity of the Escherichia coli protein StpA.
Grossberger R, Mayer O, Waldsich C, Semrad K, Urschitz S, Schroeder R., Free PMC Article | 01/21/2010 |
| crystal structure of the Escherichia coli nucleoid-associated HUalphabeta protein | Spiral structure of Escherichia coli HUalphabeta provides foundation for DNA supercoiling.
Guo F, Adhya S., Free PMC Article | 01/21/2010 |
| forms complexes with YdgT in vivo | YdgT, the Hha paralogue in Escherichia coli, forms heteromeric complexes with H-NS and StpA.
Paytubi S, Madrid C, Forns N, Nieto JM, Balsalobre C, Uhlin BE, Juárez A. | 01/21/2010 |
| StpA binding hinders DNA cleavage by both the non-specific endonuclease, DNase I, and by the site-specific type I restriction endonuclease, EcoKI. | StpA protein from Escherichia coli condenses supercoiled DNA in preference to linear DNA and protects it from digestion by DNase I and EcoKI.
Keatch SA, Leonard PG, Ladbury JE, Dryden DT., Free PMC Article | 01/21/2010 |
| Analysis of the relationship of stpA RNA chaperone activity to its RNA-binding properties. | RNA chaperone activity and RNA-binding properties of the E. coli protein StpA.
Mayer O, Rajkowitsch L, Lorenz C, Konrat R, Schroeder R., Free PMC Article | 01/21/2010 |
| StpA complements H-NS proteins defective in DNA binding to repress bgl, while in autoregulation of stpA it acts autonomously, indicating a difference in the mechanisms of repression. | Differential dependence of StpA on H-NS in autoregulation of stpA and in regulation of bgl.
Wolf T, Janzen W, Blum C, Schnetz K., Free PMC Article | 01/21/2010 |