Psu webtools
We report that IHF has high affinity for the R. A blast search currently shows homologs of IHF from other Proteobacteria: Buchnera aphidicola, Serratia marcescens, Erwinia chrysanthemi, Haemophilus influenzae, Pasteurella haemolytica, Pseudomonas aeruginosa and Pseudomonas putida of the γ subdivision and Agrobacterium tumefaciens and Rhodobacter capsulatus of the α subdivision. When phosphorylated by DctB, DctD activates transcription of dctA by catalyzing the ATP-dependent isomerization of a closed complex between Eσ 54 and the dctA promoter to an open complex that is transcriptionally competent (Lee et al., 1994, Ronson et al., 1987b).Īctivators that bind upstream of σ 54-dependent promoters are brought into proper context with the closed promoter complex via a DNA loop (Su et al., 1990, Wedel et al., 1990), which may be facilitated or hindered by the binding of IHF to a site between the UAS and σ 54-dependent promoter (for examples, see Claverie-Martin and Magasanik, 1991 and Hoover et al., 1990). DctD binds specifically and cooperatively to tandem sites in a dctA upstream activation sequence (UAS bp −94 to −154 Ledebur et al., 1990, Ledebur and Nixon, 1992, Scholl and Nixon, 1996). DctB and DctD form a two-component system which regulates transcription of the permease encoded by dctA (Ronson et al., 1987a). The dct genes of Rhizobium leguminosarum and Sinorhizobium meliloti are required for free-living cells to utilize C 4-dicarboxylates and for nitrogen fixation by the symbiotic form of these bacteria (Gu et al., 1994, Jiang et al., 1989, Ronson et al., 1981, Yarosh et al., 1989 and references cited therein). leguminosarum as a putative homolog of IHF subunit β by immunoblotting and N-terminal sequence analysis. Consistent with this hypothesis, a 12.5 kDa protein was identified from R. These data suggest that both rhizobial species have an IHF homolog that stimulates DctD-mediated transcriptional activation from the R. leguminosarum dctA that reduced the affinity of the promoter regulatory region for IHF by ∼30-fold and resulted in an eight-fold decrease in transcriptional activation in both R. A base substitution was introduced into the IHF binding site of R. Moreover, IHF had no effect on transcriptional activation from the S. leguminosarum dctA, the Sinorhizobium meliloti dctA promoter region was found to have a much weaker match to the consensus IHF binding site and a low affinity for IHF.
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leguminosarum dctA promoter both in vivo and in vitro. IHF stimulated DctD-mediated transcriptional activation from the R. IHF protected the −30 to −76 region from DNase I digestion, but systematic error in quantitative assays suggested that this protein–DNA interaction is complex.
![psu webtools psu webtools](https://www.pdx.edu/sites/g/files/znldhr781/files/TECH%20Resources%20800%20x%20530_2.jpg)
#PSU WEBTOOLS UPGRADE#
The upgrade will improve security, reduce risk and maximize the value of the University's existing contract with Microsoft.įor more information, visit the Knowledge Base article about the New Penn State Sign In.Sequence inspection identified several potential IHF binding sites adjacent to the Rhizobium leguminosarum dctA promoter.
![psu webtools psu webtools](http://img.iseephoto.com/files/photos/thumes/2016/07/over-100-internet-business-ideas-to-help-you-start-making-money-online-or-just-find-new-ways-to.jpg)
SSO allows Penn State Account holders to sign in to secure online applications with a single user ID and password.
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This change is the result of a recent upgrade to the University's single sign-on (SSO) technology.
#PSU WEBTOOLS PASSWORD#
Account holders will only need to (1) sign in with their user ID followed by the organizational identifier (e.g., (2) enter their password and (3) complete two-factor authentication (2FA) if enrolled in 2FA. The new Penn State sign-in screen will look different from WebAccess, but its functionality will remain the same. The change will remove the WebAccess login and replace it with a new Penn State Sign In provided by Microsoft to manage and secure user identities. Beginning July 7, Penn State Account holders will log in to secure University applications such as Canvas, LionPATH and Workday through a new Penn State sign-in screen by entering their Penn State user ID followed by the identifier.