The Lick AGN Monitoring Project 2016: Dynamical Modeling of Velocity-Resolved H\b{eta} Lags in Luminous Seyfert Galaxies

We have modeled the velocity-resolved reverberation response of the H\b{eta} broad emission line in nine Seyfert 1 galaxies from the Lick Active Galactic Nucleus (AGN) Monitioring Project 2016 sample, drawing inferences on the geometry and structure of the low-ionization broad-line region (BLR) and the mass of the central supermassive black hole. Overall, we find that the H\b{eta} BLR is generally a thick disk viewed at low to moderate inclination angles. We combine our sample with prior studies and investigate line-profile shape dependence, such as log10(FWHM/{\sigma}), on BLR structure and kinematics and search for any BLR luminosity-dependent trends. We find marginal evidence for an anticorrelation between the profile shape of the broad H\b{eta} emission line and the Eddington ratio, when using the root-mean-square spectrum. However, we do not find any luminosity-dependent trends, and conclude that AGNs have diverse BLR structure and kinematics, consistent with the hypothesis of transient AGN/BLR conditions rather than systematic trends

The Lick AGN Monitoring Project 2016 : dynamical modeling of velocity-resolved Hβ lags in luminous Seyfert galaxies

K.H. acknowledges support from STFC grant ST/R000824/1.We have modeled the velocity-resolved reverberation response of the Hβ broad emission line in nine Seyfert 1 galaxies from the Lick Active Galactic Nucleus (AGN) Monitoring Project 2016 sample, drawing inferences on the geometry and structure of the low-ionization broad-line region (BLR) and the mass of the central supermassive black hole. Overall, we find that the Hβ BLR is generally a thick disk viewed at low to moderate inclination angles. We combine our sample with prior studies and investigate line-profile shape dependence, such as log10(FWHM/σ), on BLR structure and kinematics and search for any BLR luminosity-dependent trends. We find marginal evidence for an anticorrelation between the profile shape of the broad Hβ emission line and the Eddington ratio, when using the rms spectrum. However, we do not find any luminosity-dependent trends, and conclude that AGNs have diverse BLR structure and kinematics, consistent with the hypothesis of transient AGN/BLR conditions rather than systematic trends.Publisher PDFPeer reviewe

The Lick AGN Monitoring Project 2016 : velocity-resolved Hβ lags in luminous Seyfert galaxies

Funding: K.H. acknowledges support from STFC grant ST/R000824/1.We carried out spectroscopic monitoring of 21 low-redshift Seyfert 1 galaxies using the Kast double spectrograph on the 3 m Shane telescope at Lick Observatory from April 2016 to May 2017. Targetingactive galactic nuclei (AGN) with luminosities of λLλ(5100 Å) ≈ 1044 erg s−1 and predicted Hβ lags of∼ 20–30 days or black hole masses of 107–108.5 M⊙, our campaign probes luminosity-dependent trends in broad-line region (BLR) structure and dynamics as well as to improve calibrations for single-epoch estimates of quasar black hole masses. Here we present the first results from the campaign, including Hβ emission-line light curves, integrated Hβ lag times (8–30 days) measured against V -band continuum light curves, velocity-resolved reverberation lags, line widths of the broad Hβ components, and virial black hole mass estimates (107.1–108.1 M⊙). Our results add significantly to the number of existing velocity-resolved lag measurements and reveal a diversity of BLR gas kinematics at moderately high AGN luminosities. AGN continuum luminosity appears not to be correlated with the type of kinematics that its BLR gas may exhibit. Follow-up direct modeling of this dataset will elucidate the detailed kinematics and provide robust dynamical black hole masses for several objects in this sample.Publisher PDFPeer reviewe

Further characterization of the interaction between the cytoskeletal proteins talin and vinculin.

The cytoskeletal protein talin, which is thought to couple integrins to F-actin, contains three binding sites (VBS1-VBS3) for vinculin, a protein implicated in the negative regulation of cell motility and whose activity is modulated by an intramolecular interaction between the vinculin head (Vh) and vinculin tail (Vt) domains. In the present study we show that recombinant talin polypeptides containing the three VBSs (VBS1, residues 498-636; VBS2, residues 727-965; and VBS3, residues 1943-2157) each bind tightly to the same or overlapping sites within vinculin(1-258). A short synthetic talin VBS3 peptide (residues 1944-1969) was sufficient to inhibit binding of a (125)I-labelled talin VBS3 polypeptide to vinculin(1-258), and NMR spectroscopy confirmed that this peptide forms a 1:1 complex in slow exchange with vinculin(1-258). Binding of the (125)I-labelled VBS3 polypeptide was markedly temperature dependent, but was not inhibited by 1 M salt or 10% (v/v) 2-methyl-2-propanol. Attempts to further define the talin-binding site within vinculin(1-258) using a gel-blot assay were unsuccessful, but near maximal talin-binding activity was retained by a construct spanning vinculin residues 1-131 in a yeast two-hybrid assay. Interestingly, the talin VBS3 polypeptide was a potent inhibitor of the Vh-Vt interaction, and the VBS3 synthetic peptide was able to expose the actin-binding site in intact vinculin, which is otherwise masked by the Vh-Vt interaction. The results suggest that under certain conditions, talin may be an effective activator of vinculin

Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle

The interaction between the cytoskeletal proteins talin and vinculin plays a key role in integrin-mediated cell adhesion and migration. We have determined the crystal structures of two domains from the talin rod spanning residues 482–789. Talin 482–655, which contains a vinculin-binding site (VBS), folds into a five-helix bundle whereas talin 656–789 is a four-helix bundle. We show that the VBS is composed of a hydrophobic surface spanning five turns of helix 4. All the key side chains from the VBS are buried and contribute to the hydrophobic core of the talin 482–655 fold. We demonstrate that the talin 482–655 five-helix bundle represents an inactive conformation, and mutations that disrupt the hydrophobic core or deletion of helix 5 are required to induce an active conformation in which the VBS is exposed. We also report the crystal structure of the N-terminal vinculin head domain in complex with an activated form of talin. Activation of the VBS in talin and the recruitment of vinculin may support the maturation of small integrin/talin complexes into more stable adhesions