ABSTRACT
Isolated pyramids, 30-80 nm wide and 3-20 nm tall, form during sputter-annealing cycles on the Ge (110) surface. Pyramids have four walls with {19 13 1} faceting and a steep mound at the apex. We used scanning tunneling microscopy (STM) under ultrahigh vacuum conditions to periodically image the surface at ion energies between 100 eV and 500 eV and incremental total flux. Pyramids are seen using Ar+ between 200 eV and 400 eV, and require Ag to be present on the sample or sample holder. We suspect that the pyramids are initiated by Ag co-sputtered onto the surface. Growth of pyramids is due to the gathering of step edges with (16 × 2) reconstruction around the pyramid base during layer-by-layer removal of the substrate, and conversion to {19 13 1} faceting. The absence of pyramids using Ar+ energies above 400 eV is likely due to surface damage that is insufficiently annealed.
ABSTRACT
We identified the interaction between HBV X (HBx) protein and the oncogene AIB1 (amplified in breast cancer 1). A serine/proline motif (SSPSPS) in HBx was found to be required for the interaction. Two LXD motifs [LLXX(X)L, X means any amino acids], LLRNSL and LLDQLHTLL in AIB1 were also found to be involved in the HBx-AIB1 interaction. The HBx-AIB1 interaction was important for the activation of NFκB signal transduction, the HBx mutant that did not interact with AIB1showed dramatically lower NFκB activation activity than the WT HBx. These findings contribute to the new understanding on signal transduction activation mechanisms of HBx.
Subject(s)
Carcinogens , NF-kappa B/metabolism , Nuclear Receptor Coactivator 3/metabolism , Trans-Activators/metabolism , Amino Acid Sequence , Carcinoma, Hepatocellular/genetics , Carcinoma, Hepatocellular/metabolism , Cell Line, Tumor , Conserved Sequence , Humans , Molecular Sequence Data , Mutation , Nuclear Receptor Coactivator 3/genetics , Protein Interaction Domains and Motifs , Serine/genetics , Serine/metabolism , Signal Transduction , Trans-Activators/genetics , Two-Hybrid System Techniques , Viral Regulatory and Accessory ProteinsABSTRACT
The T:G mismatch specific DNA glycosylase (TDG) is known as an important enzyme in repairing damaged DNA. Recent studies also showed that TDG interacts with a p160 protein, steroid receptor coactivator 1 or nuclear receptor coactivator 1 (SRC1), and is involved in transcriptional activation of the estrogen receptor. However, whether other members of the p160 family are also involved in TDG-interaction and signal transduction regulation remains to be seen. In this study, we employed the mammalian two-hybrid system to investigate the interaction between TDG and another member of the p160 family, nuclear receptor coactivator 3 (NCoA-3). We found that a DXXD motif from aa 294-297 within TDG was responsible for the TDG-NCoA-3 interaction, we also found that a LLXXXL motif (X means any amino acid) from aa 1029-1037 (LLRNSL) and a merged LLXXL motif (LLDQLHTLL) from aa 1053-1061 in NCoA-3 were important for the TDG-NCoA-3 interactions. Mutation of the two aspartic acids (aa 294 and 297) into two alanines in TDG significantly affected the interaction and subsequent transcriptional activation of several steroid hormone receptors including, estrogen-, androgen- and progesterone- receptors in Huh7 cells. We also identified that mutations of NCoA-3 at either leucines 1029-1030 or 1053-1054 (replaced by alanines) also reduced the interaction activity between TDG and NCoA1. These data indicated that the TDG-NCoA-3 interaction is important for broad range activation of steroid hormone nuclear receptors, and may also contribute significantly to further understanding of TDG-related nuclear receptor regulation.
