| 1. |
|
|
| 2. |
- Grönroos, Eva, et al.
(författare)
-
Control of Smad7 stability by competition between acetylation and ubiquitination
- 2002
-
Ingår i: Molecular Cell. - 1097-2765 .- 1097-4164. ; 10:3, s. 483-493
-
Tidskriftsartikel (refereegranskat)abstract
- Smad proteins regulate gene expression in response to TGFbeta signaling. Here we present evidence that Smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of Smad7 on two lysine residues in its N terminus. Acetylation or mutation of these lysine residues stabilizes Smad7 and protects it from TGFbeta-induced degradation. Furthermore, we demonstrate that the acetylated residues in Smad7 also are targeted by ubiquitination and that acetylation of these lysine residues prevents subsequent ubiquitination. Specifically, acetylation of Smad7 protects it against ubiquitination and degradation mediated by the ubiquitin ligase Smurf1. Thus, our data suggest that competition between ubiquitination and acetylation of overlapping lysine residues constitutes a novel mechanism to regulate protein stability.
|
|
| 3. |
- Dellino, Gaetano I, et al.
(författare)
-
Polycomb silencing blocks transcription initiation.
- 2004
-
Ingår i: Molecular Cell. - 1097-2765 .- 1097-4164. ; 13:6, s. 887-93
-
Tidskriftsartikel (refereegranskat)abstract
- Polycomb (PcG) complexes maintain the silent state of target genes. The mechanism of silencing is not known but has been inferred to involve chromatin packaging to block the access of transcription factors. We have studied the effect of PcG silencing on the hsp26 heat shock promoter. While silencing does decrease the accessibility of some restriction enzyme sites to some extent, it does not prevent the binding of TBP, RNA polymerase, or the heat shock factor to the hsp26 promoter, as shown by chromatin immunoprecipitation. However, we find that in the repressed state, the RNA polymerase cannot initiate transcription. We conclude that, rather than altering chromatin structure to block accessibility, PcG silencing in this construct targets directly the activity of the transcriptional machinery at the promoter.
|
|
| 4. |
- Nissan, Tracy A, et al.
(författare)
-
A pre-ribosome with a tadpole-like structure functions in ATP-dependent maturation of 60S subunits
- 2004
-
Ingår i: Molecular Cell. - : Elsevier BV. - 1097-2765 .- 1097-4164. ; 15:2, s. 295-301
-
Tidskriftsartikel (refereegranskat)abstract
- Analyses of isolated pre-ribosomes yielded biochemical "snapshots" of the dynamic, nascent 60S and 40S subunits during their path from the nucleolus to the cytoplasm. Here, we present the structure of a pre-60S ribosomal intermediate located in the nucleoplasm. A huge dynein-related AAA-type ATPase (Rea1) and the Rix1 complex (Rix1-Ipi1-Ipi3) are components of an extended (approximately 45 nm long) pre-60S particle. Antibody crosslinking in combination with electron microscopy revealed that the Rea1 localizes to the "tail" region and ribosomal proteins to the "head" region of the elongated "tadpole-like" structure. Furthermore, in vitro treatment with ATP induces dissociation of Rea1 from the pre-60S subunits. Rea1 and the Rix1 complex could mediate ATP-dependent remodeling of 60S subunits and subsequent export from the nucleoplasm to the cytoplasm.
|
|
| 5. |
- Novak, R, et al.
(författare)
-
Signal transduction by a death signal peptide : uncovering the mechanism of bacterial killing by penicillin.
- 2000
-
Ingår i: Molecular Cell. - 1097-2765 .- 1097-4164. ; 5:1, s. 49-57
-
Tidskriftsartikel (refereegranskat)abstract
- The binding of bactericidal antibiotics like penicillins, cephalosporins, and glycopeptides to their bacterial targets stops bacterial growth but does not directly cause cell death. A second process arising from the bacteria itself is necessary to trigger endogenous suicidal enzymes that dissolve the cell wall during autolysis. The signal and the trigger pathway for this event are completely unknown. Using S. pneumoniae as a model, we demonstrate that signal transduction via the two-component system VncR/S triggers multiple death pathways. We show that the signal sensed by VncR/S is a secreted peptide, Pep27, that initiates the cell death program. These data depict a novel model for the control of bacterial cell death.
|
|
| 6. |
|
|
| 7. |
|
|
| 8. |
- Lorch, Y, et al.
(författare)
-
Mediator-nucleosome interaction
- 2000
-
Ingår i: Molecular cell. - 1097-2765. ; 6:1, s. 197-201
-
Tidskriftsartikel (refereegranskat)
|
|
| 9. |
|
|
| 10. |
|
|
