Kinetic studies of anthracycline-DNA interaction by fluorescence stopped flow confirm a complex association mechanism

Biochemistry ◽  
1989 ◽  
Vol 28 (1) ◽  
pp. 274-282 ◽  
Author(s):  
Vincenzo Rizzo ◽  
Nereo Sacchi ◽  
Milena Menozzi
Keyword(s):  
Kinetic Studies ◽  
Dna Interaction ◽  
Stopped Flow

scholarly journals Real-time kinetic studies of Mycobacterium tuberculosis LexA-DNA interaction

2021 ◽  
Author(s):  
Chitral Chatterjee ◽  
Soneya Majumdar ◽  
Sachin Deshpande ◽  
Deepak Pant ◽  
Saravanan Matheshwaran
Keyword(s):  
Amino Acids ◽  
Mycobacterium Tuberculosis ◽  
Dna Binding ◽  
Kinetic Parameters ◽  
Dna Sequences ◽  
Kinetic Studies ◽  
Dna Interaction ◽  
Damage Repair ◽  
Inducible Genes ◽  
Kinetics Of

Transcriptional repressor, LexA, regulates the “SOS” response, an indispensable bacterial DNA damage repair machinery.  Compared to its E.coli ortholog, LexA from Mycobacterium tuberculosis (Mtb) possesses a unique N-terminal extension of additional 24 amino acids in its DNA binding domain (DBD) and 18 amino acids insertion at its hinge region that connects the DBD to the C-terminal dimerization/autoproteolysis domain. Despite the importance of LexA in “SOS” regulation, Mtb LexA remains poorly characterized and the functional importance of its additional amino acids remained elusive. In addition, the lack of data on kinetic parameters of Mtb LexA-DNA interaction prompted us to perform kinetic analyses of Mtb LexA and its deletion variants using Bio-layer Interferometry (BLI). Mtb LexA is seen to bind to different “SOS” boxes, DNA sequences present in the operator regions of damage-inducible genes, with comparable nanomolar affinity. Deletion of 18 amino acids from the linker region is found to affect DNA binding unlike the deletion of the N-terminal stretch of extra 24 amino acids. The conserved RKG motif has been found to be critical for DNA binding. Overall, this study provides insights into the kinetics of the interaction between Mtb LexA and its target “SOS” boxes. The kinetic parameters obtained for DNA binding of Mtb LexA would be instrumental to clearly understand the mechanism of “SOS” regulation and activation in Mtb.

scholarly journals Kinetic Studies of the Interaction of Toluidine Blue with Poly-(αL-glutamic acid) by Means of Stopped-Flow Method

1978 ◽  
Vol 10 (2) ◽  
pp. 153-159 ◽  
Author(s):  
Hidetoshi Ushio ◽  
Hiroshi Uchimura ◽  
Yoshikuni Tsuji ◽  
Takayuki Sano ◽  
Tatsuya Yasunaga
Keyword(s):  
Glutamic Acid ◽  
Toluidine Blue ◽  
Kinetic Studies ◽  
Stopped Flow ◽  
Flow Method

Stopped flow kinetic studies on reductive half-reaction of histamine dehydrogenase from Nocardioides simplex with histamine

2010 ◽  
Vol 148 (1) ◽  
pp. 47-54
Author(s):  
Maiko Tsutsumi ◽  
Seiya Tsujimura ◽  
Osamu Shirai ◽  
Kenji Kano
Keyword(s):  
Kinetic Studies ◽  
Stopped Flow

Kinetic studies with a stopped-flow spectrograph

1976 ◽  
Vol 9 (9) ◽  
pp. 787-789 ◽  
Author(s):  
P J Benson ◽  
P Moore
Keyword(s):  
Kinetic Studies ◽  
Stopped Flow

Kinetic studies on the reaction between copper(II) ions and some dithiocarbonates using stopped-flow technique

2003 ◽  
Vol 6 (1) ◽  
pp. 54-57 ◽  
Author(s):  
N.D. Yordanov ◽  
V. Gancheva ◽  
B. Mladenova ◽  
G. Grampp
Keyword(s):  
Kinetic Studies ◽  
Stopped Flow
Sign in / Sign up

Export Citation Format

Share Document