Femtosecond Photoisomerization Study on Azobenzene-Derivative Bound by DNA

2010 ◽  
Author(s):  
T. Chen ◽  
K. Igarashi ◽  
A. Yamaguchi ◽  
N. Nakagawa ◽  
K. Yamane ◽  
...  
Keyword(s):  
Derivative Bound

Structure of a 7,12-dimethylbenz[a]anthracene 5,6-oxide derivative bound to C-8 of guanosine

1980 ◽  
pp. 82 ◽  
Author(s):  
Koji Nakanishi ◽  
Hajime Komura ◽  
Iwao Miura ◽  
Hiroshi Kasai ◽  
Krystyna Frenkel ◽  
...  
Keyword(s):  
Derivative Bound ◽  
Oxide Derivative

Regulation of Redox Potential of a Pterin Derivative Bound to a Ruthenium(II) Complex by Intermolecular Hydrogen Bonding with Nucleobases

2012 ◽  
Vol 124 (19) ◽  
pp. 4701-4705 ◽  
Author(s):  
Yuji Inui ◽  
Soushi Miyazaki ◽  
Kei Ohkubo ◽  
Shunichi Fukuzumi ◽  
Takahiko Kojima
Keyword(s):  
Hydrogen Bonding ◽  
Redox Potential ◽  
Intermolecular Hydrogen Bonding ◽  
Derivative Bound

FLUORESCENCE STUDY OF THE PHYSICO-CHEMICAL PROPERTIES OF A BENZO(A)PYRENE7,8-DIHYDRODIOL9,10-OXIDE DERIVATIVE BOUND COVALENTLY TO DNA

1979 ◽  
Vol 29 (2) ◽  
pp. 223-232 ◽  
Author(s):  
Thaddeus Prusik ◽  
Nicholas E. Geacintov ◽  
Christopher Tobiasz ◽  
Vesna Ivanovic ◽  
I. Bernard Weinstein
Keyword(s):  
Chemical Properties ◽  
Fluorescence Study ◽  
Physico Chemical ◽  
Derivative Bound ◽  
Oxide Derivative

scholarly journals The central part of the 5.8 S rRNA is differently arranged in programmed and free human ribosomes

2005 ◽  
Vol 387 (1) ◽  
pp. 139-145 ◽  
Author(s):  
Dmitri GRAIFER ◽  
Maxim MOLOTKOV ◽  
Anna EREMINA ◽  
Aliya VEN'YAMINOVA ◽  
Marina REPKOVA ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Ribosomal Proteins ◽  
Cross Linking ◽  
Rrna Sequence ◽  
Conformational Switch ◽  
Cryo Electron Microscopy ◽  
Initiation Of Translation ◽  
The Difference ◽  
Derivative Bound ◽  
Microscopy Images

A sequence-specific modification of the human 5.8 S rRNA in isolated 60 S subunits, non-programmed 80 S ribosomes and ribosomes complexed with mRNA and tRNAs was studied with the use of a derivative of the nonaribonucleotide UCUGUGUUU bearing a perfluorophenylazide group on the C-5 atom of the 5′-terminal uridine. Part of the oligonucleotide moiety of the derivative was complementary to the 5.8 S rRNA sequence ACACA in positions 82–86 flanked by two guanines at the 5′-terminus. The target for the cross-linking was identified as nucleotide G89 on the 5.8 S RNA. In addition, several ribosomal proteins were modified by the oligonucleotide derivative bound to the 5.8 S rRNA and proteins L6 and L8 were among them. Application of these results to known cryo-electron microscopy images of eukaryotic 60 S subunits made it possible to suggest that the central part of the 5.8 S rRNA containing the sequence 82–86 and proteins L6 and L8 are located at the base of the L1 stalk of the 60 S subunit. The efficacy of cross-linking in non-programmed 80 S ribosomes was much lower than in isolated 60 S subunits and in programmed 80 S ribosomes. We suggest that the difference in the accessibilities of the central part of the 5.8 S rRNA in the programmed and non-programmed 80 S ribosomes is caused by a conformational switch that seems to be required to dissociate the 80 S ribosomes into the subunits after termination of translation to allow initiation of translation of a new template.

Effect of octabromination of a tetrakis(4-carboxyphenyl)porphine derivative bound to silica gels on HPLC retention behaviors of polyaromatic hydrocarbons

Talanta ◽  
2006 ◽  
Vol 69 (5) ◽  
pp. 1260-1264 ◽  
Author(s):  
Youji Kitamura ◽  
Kenji Kawata ◽  
Kurumi Tanaka ◽  
Yuko Furuyashiki ◽  
Masaki Mifune ◽  
...  
Keyword(s):  
Polyaromatic Hydrocarbons ◽  
Silica Gels ◽  
Derivative Bound

scholarly journals Disease-associated mutation in SRSF2 misregulates splicing by altering RNA-binding affinities

2015 ◽  
Vol 112 (34) ◽  
pp. E4726-E4734 ◽  
Author(s):  
Jian Zhang ◽  
Yen K. Lieu ◽  
Abdullah M. Ali ◽  
Alex Penson ◽  
Kathryn S. Reggio ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Rna Binding ◽  
Splicing Factors ◽  
Binding Affinities ◽  
Protein Protein Interactions ◽  
Mrna Isoforms ◽  
Exon Inclusion ◽  
Wild Type Counterpart ◽  
Derivative Bound ◽  
Shed Light

Serine/arginine-rich splicing factor 2 (SRSF2) is an RNA-binding protein that plays important roles in splicing of mRNA precursors. SRSF2 mutations are frequently found in patients with myelodysplastic syndromes and certain leukemias, but how these mutations affect SRSF2 function has only begun to be examined. We used clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR-associated protein-9 nuclease to introduce the P95H mutation to SRSF2 in K562 leukemia cells, generating an isogenic model so that splicing alterations can be attributed solely to mutant SRSF2. We found that SRSF2 (P95H) misregulates 548 splicing events (<1% of total). Of these events, 374 involved the inclusion of cassette exons, and the inclusion was either increased (206) or decreased (168). We detected a specific motif (UCCA/UG) enriched in the more-included exons and a distinct motif (UGGA/UG) in the more-excluded exons. RNA gel shift assays showed that a mutant SRSF2 derivative bound more tightly than its wild-type counterpart to RNA sites containing UCCAG but bound less tightly to UGGAG sites. Thus in most cases the pattern of exon inclusion or exclusion correlated with stronger or weaker RNA binding, respectively. We further show that the P95H mutation does not affect other functions of SRSF2, i.e., protein–protein interactions with key splicing factors. Our results thus demonstrate that the P95H mutation positively or negatively alters the binding affinity of SRSF2 for cognate RNA sites in target transcripts, leading to misregulation of exon inclusion. Our findings shed light on the mechanism of the disease-associated SRSF2 mutation in splicing regulation and also reveal a group of misspliced mRNA isoforms for potential therapeutic targeting.

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