Conformational studies of a peptide corresponding to a region of the C-terminus of ribonuclease A: implications as a potential chain-folding initiation site

Biochemistry ◽  
1991 ◽  
Vol 30 (31) ◽  
pp. 7680-7692 ◽  
Author(s):  
John M. Beals ◽  
Elisha Haas ◽  
Sara Krausz ◽  
Harold A. Scheraga
Keyword(s):  
Initiation Site ◽  
Ribonuclease A ◽  
Conformational Studies ◽  
Chain Folding ◽  
C Terminus

Comparison of Heat- and Pressure-Induced Unfolding of Ribonuclease A:  The Critical Role of Phe46 Which Appears To Belong to a New Hydrophobic Chain-Folding Initiation Site†

Biochemistry ◽  
2002 ◽  
Vol 41 (14) ◽  
pp. 4567-4574 ◽  
Author(s):  
Eri Chatani ◽  
Kazuhiko Nonomura ◽  
Rikimaru Hayashi ◽  
Claude Balny ◽  
Reinhard Lange
Keyword(s):  
Critical Role ◽  
Initiation Site ◽  
Ribonuclease A ◽  
Chain Folding ◽  
Hydrophobic Chain

Pressure versus Heat-Induced Unfolding of Ribonuclease A:  The Case of Hydrophobic Interactions within a Chain-Folding Initiation Site†

Biochemistry ◽  
1999 ◽  
Vol 38 (48) ◽  
pp. 15952-15961 ◽  
Author(s):  
Joan Torrent ◽  
James Patrick Connelly ◽  
Maria Gràcia Coll ◽  
Marc Ribó ◽  
Reinhard Lange ◽  
...  
Keyword(s):  
Hydrophobic Interactions ◽  
Initiation Site ◽  
Ribonuclease A ◽  
Chain Folding ◽  
A Chain

Valine 108, a Chain-Folding Initiation Site-Belonging Residue, Crucial for the Ribonuclease A Stability

1999 ◽  
Vol 265 (2) ◽  
pp. 356-360 ◽  
Author(s):  
M.G. Coll ◽  
I.I. Protasevich ◽  
J. Torrent ◽  
M. Ribó ◽  
V.M. Lobachov ◽  
...  
Keyword(s):  
Initiation Site ◽  
Ribonuclease A ◽  
Chain Folding ◽  
A Chain

scholarly journals Sir3p Domains Involved in the Initiation of Telomeric Silencing in Saccharomyces cerevisiae

Genetics ◽  
1998 ◽  
Vol 150 (3) ◽  
pp. 977-986 ◽  
Author(s):  
Yangsuk Park ◽  
John Hanish ◽  
Arthur J Lustig
Keyword(s):  
Amino Acids ◽  
Active Site ◽  
Fusion Proteins ◽  
Initiation Site ◽  
Negative Control ◽  
Model System ◽  
Mutant Protein ◽  
Regulatory Domain ◽  
C Terminus ◽  
Necessary And Sufficient

Abstract Previous studies from our laboratory have demonstrated that tethering of Sir3p at the subtelomeric/telomeric junction restores silencing in strains containing Rap1-17p, a mutant protein unable to recruit Sir3p. This tethered silencing assay serves as a model system for the early events that follow recruitment of silencing factors, a process we term initiation. A series of LexA fusion proteins in-frame with various Sir3p fragments were constructed and tested for their ability to support tethered silencing. Interestingly, a region comprising only the C-terminal 144 amino acids, termed the C-terminal domain (CTD), is both necessary and sufficient for restoration of silencing. Curiously, the LexA-Sir3N205 mutant protein overcomes the requirement for the CTD, possibly by unmasking a cryptic initiation site. A second domain spanning amino acids 481-835, termed the nonessential for initiation domain (NID), is dispensable for the Sir3p function in initiation, but is required for the recruitment of the Sir4p C terminus. In addition, in the absence of the N-terminal 481 amino acids, the NID negatively influences CTD activity. This suggests the presence of a third region, consisting of the N-terminal half (1-481) of Sir3p, termed the positive regulatory domain (PRD), which is required to initiate silencing in the presence of the NID. These data suggest that the CTD “active” site is under both positive and negative control mediated by multiple Sir3p domains.

Chain-folding initiation structures in ribonuclease A: conformational analysis of trans-Ac-Asn-Pro-Tyr-NHMe and trans-Ac-Tyr-Pro-Asn-NHMe in water and in the solid state

1984 ◽  
Vol 106 (25) ◽  
pp. 7959-7969 ◽  
Author(s):  
G. T. Montelione ◽  
E. Arnold ◽  
Y. C. Meinwald ◽  
E. R. Stimson ◽  
J. B. Denton ◽  
...  
Keyword(s):  
Solid State ◽  
Conformational Analysis ◽  
Ribonuclease A ◽  
Chain Folding

Chain folding in ribonuclease A derivatives lacking five and six carboxyl-terminal residues

Biochemistry ◽  
1972 ◽  
Vol 11 (23) ◽  
pp. 4304-4307 ◽  
Author(s):  
David Puett ◽  
Elaine Friebele ◽  
Betty Kay Wasserman
Keyword(s):  
Ribonuclease A ◽  
Chain Folding ◽  
Carboxyl Terminal

Structure and dynamics of chain-folding initiation sites in ribonuclease A

1992 ◽  
Author(s):  
Harold A. Scheraga ◽  
J. M. Beals ◽  
D. R. Buckler ◽  
Elisha Haas ◽  
S. Krausz
Keyword(s):  
Ribonuclease A ◽  
Chain Folding ◽  
Structure And Dynamics

scholarly journals Human U2 snRNA Genes Exhibit a Persistently Open Transcriptional State and Promoter Disassembly at Metaphase

2008 ◽  
Vol 28 (11) ◽  
pp. 3573-3588 ◽  
Author(s):  
Thomas Pavelitz ◽  
Arnold D. Bailey ◽  
Christopher P. Elco ◽  
Alan M. Weiner
Keyword(s):  
Chromatin Immunoprecipitation ◽  
Actinomycin D ◽  
Chromatin Condensation ◽  
Initiation Site ◽  
Coding Region ◽  
Sequence Element ◽  
U2 Snrna ◽  
Proximal Sequence Element ◽  
C Terminus ◽  
Transcriptional State

ABSTRACT In mammals, small multigene families generate spliceosomal U snRNAs that are nearly as abundant as rRNA. Using the tandemly repeated human U2 genes as a model, we show by footprinting with DNase I and permanganate that nearly all sequences between the enhancer-like distal sequence element and the initiation site are protected during interphase whereas the upstream half of the U2 snRNA coding region is exposed. We also show by chromatin immunoprecipitation that the SNAPc complex, which binds the TATA-like proximal sequence element, is removed at metaphase but remains bound under conditions that induce locus-specific metaphase fragility of the U2 genes, such as loss of CSB, BRCA1, or BRCA2 function, treatment with actinomycin D, or overexpression of the tetrameric p53 C terminus. We propose that the U2 snRNA promoter establishes a persistently open state to facilitate rapid reinitiation and perhaps also to bypass TFIIH-dependent promoter melting; this open state would then be disassembled to allow metaphase chromatin condensation.

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