The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II

Molecular Cell

Volumn 7, Issue 5, 2001, Pages 981-991

  Ferdous, Anwarul ^a   Gonzalez, Fernando ^a   Sun, Liping ^a   Kodadek, Thomas ^a   Johnston, Stephen Albert ^a  

^a UNIVERSITY OF TEXAS AT DALLAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AZAURACIL; ELONGATION FACTOR; ELONGATION FACTOR CDC 68; PROTEASOME; RNA POLYMERASE II; UNCLASSIFIED DRUG;

ALLELE; ARTICLE; ENZYME SUBUNIT; PHENOTYPE; PROTEIN DEGRADATION; RNA TRANSCRIPTION; RNA TRANSLATION; YEAST;

EID: 0035947238     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(01)00250-7     Document Type: Article

References (58)

1. The proteasome: Paradigm of a self-compartmentalizing protease
2. The base of the proteasome regulatory particle exhibits chaperone-like activity
3. The basics of basal transcription by RNA polymerase II
4. Control of elongation by RNA polymerase II
5. General initiation factors for RNA polymerase II
6. A 200 amino acid ATPase module in search of a basic function
7. Structure and function of the 20S and 26S proteasomes
8. 6-Azauricil inhibition of GTP biosynthesis in Saccharomyces cerevisiae
9. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
10. SUG1, a putative transcriptional mediator and subunit of the PA700 proteasome regulatory complex, is a DNA helicase
11. The regulatory particle of the Saccharomyces cerevisiae proteasome
12. Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins
13. Identification and analysis of a functional human homolog of the SPT4 gene of Saccharomyces cerevisiae
14. Evidence that Spt4, Spt5 and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae
15. PRE2, highly homologous to the human major histocompatability complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins
16. The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity
17. Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP
18. Met30-mediated inactivation of the transcription factor Met4
19. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
20. Requirement of RSF and FACT for transcription of chromatin templates in vitro
21. Mutations in SPT16/CDC68 suppress cis- and trans-acting mutations that affect promoter function in Saccharomyces cerevisiae
22. Control of RNA polymerase II elogation potential by a novel carboxyl-terminal domain kinase
23. Proteasome-mediated degradation of the vitamin D receptor (VDR) and a putative role for SUG1 interaction with the AF-2 domain of VDR
24. Proteasome-mediated degradation of transcriptional activators correlates with activation domain potency in vivo
25. Ubiquitination of RNA polymerase II large subunit signaled by phosphorylation of carboxyl-terminal domain
26. Nonproteolytic function of the proteasome is required for the dissociation of Cdc2 and cyclin B at the end of M phase
27. The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins
28. The highly conserved, coregulated SNO and SNZ gene families in Saccharomyces cerevisiae respond to nutrient limitation
29. Mutations in the second largest subunit of RNA polymerase II cause 6-azauricil sensitivity in yeast and increased transcriptional arrest in vitro
30. The RNA polymerase II general elongation factors
31. The role of general initiation factors in transcription by RNA polymerase II
32. CDC68, a yeast gene that affects regulation of cell proliferation and transcription, encodes a protein with a highly acidic carboxyl terminus
33. Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome
34. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
35. Evidence that proteolysis of Gal4 can not explain the transcriptional effects of proteasome ATPase mutations
36. The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair
37. Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26S proteasome
38. Subcellular localization, stoichiometry, and protein levels of 26S proteasome subunits in yeast
39. Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis
40. Rad23 links DNA repair to the ubiquitin/proteasome pathway
41. Saccharomyces cerevisiae transcription elongation mutants are defective in PUR5 induction in response to nucleotide depletion
42. Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP
43. Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26S proteasome
44. Alterations in a yeast protein resembling HIV Tat-binding protein relieve the requirement for an acidic activation domain of GAL4
45. Highly conserved ATPase protein as mediator between acidic activation domains and the TATA-binding protein
46. Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
47. FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH
48. DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs
49. A small amphipathic α-helical region is required for transcriptional activities and proteasome-dependent turnover of the tyrosine-phosphorylated Stat5
50. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
51. The XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factor
52. The Saccharomyces cerevisiae DNA polymerase α catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG-1-like protein
53. Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase α
54. Accurate initiation by RNA polymerase II in a whole cell extract from Saccharomyces cerevisiae
55. Sug1 modulates yeast transcription by Cdc68
56. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation
57. The nucleic acid binding activity of bleomycin hydrolase is involved in bleomycin detoxification
58. The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase