scholarly journals Fluorescent substrate analog for monitoring chain elongation by undecaprenyl pyrophosphate synthase in real time

2011 ◽  
Vol 417 (1) ◽  
pp. 136-141 ◽  
Author(s):  
Kuo-Hsun Teng ◽  
Annie P.-C. Chen ◽  
Chih-Jung Kuo ◽  
Yu-Chin Li ◽  
Hon-Ge Liu ◽  
...  
Keyword(s):  
Real Time ◽  
Chain Elongation ◽  
Fluorescent Substrate ◽  
Substrate Analog

scholarly journals Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli.

1996 ◽  
Vol 40 (7) ◽  
pp. 1640-1644 ◽  
Author(s):  
P E Brandish ◽  
K I Kimura ◽  
M Inukai ◽  
R Southgate ◽  
J T Lonsdale ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antibacterial Agents ◽  
Enzyme Assay ◽  
Molecular Mechanisms ◽  
Fluorescent Substrate ◽  
Acceptor Substrate ◽  
Nucleoside Antibiotics ◽  
Substrate Analog ◽  
Binding Inhibition ◽  
Insight Into

Using a continuous fluorescence-based enzyme assay, we have characterized the antibacterial agents tumicamycin and liposidomycin B as inhibitors of solubilized Escherichia coli phospho-N-acetylmuramyl-pentapeptide translocase. Tunicamycin exhibited reversible inhibition (Ki = 0.55 +/- 0.1 microM) which was noncompetitive with respect to the lipid acceptor substrate and competitive with respect to the fluorescent substrate analog, dansyl-UDPMurNAc-pentapeptide. Liposidomycin B exhibited slow-binding inhibition (Ki = 80 +/- 15 nM) which was competitive with respect to the lipid acceptor substrate and noncompetitive with respect to dansyl-UDPMurNAc-pentapeptide. These results provide insight into the molecular mechanisms of action of these two classes of nucleoside antibiotics.

scholarly journals Real-time, spatially resolved analysis of serotonin transporter activity and regulation using the fluorescent substrate, ASP+

2010 ◽  
pp. no-no ◽  
Author(s):  
Murat Oz ◽  
Therissa Libby ◽  
Bronwyn Kivell ◽  
Vanaja Jaligam ◽  
Sammanda Ramamoorthy ◽  
...  
Keyword(s):  
Real Time ◽  
Serotonin Transporter ◽  
Fluorescent Substrate ◽  
Spatially Resolved

Fluorescent substrate analog for adenosine deaminase: 3'-O-[5-(dimethylamino)naphthalene-1-sulfonyl]adenosine

Biochemistry ◽  
1981 ◽  
Vol 20 (11) ◽  
pp. 3103-3109 ◽  
Author(s):  
Gedalyahu Skorka ◽  
Pessia Shuker ◽  
David Gill ◽  
Jacob Zabicky ◽  
Abraham H. Parola
Keyword(s):  
Adenosine Deaminase ◽  
Fluorescent Substrate ◽  
Substrate Analog

scholarly journals Real-time Imaging ofMycobacterium tuberculosis, Using a Novel Near-Infrared Fluorescent Substrate

2016 ◽  
pp. jiw298 ◽  
Author(s):  
Hee-Jeong Yang ◽  
Ying Kong ◽  
Yunfeng Cheng ◽  
Harish Janagama ◽  
Hany Hassounah ◽  
...  
Keyword(s):  
Real Time ◽  
Near Infrared ◽  
Fluorescent Substrate ◽  
Real Time Imaging ◽  
Ofmycobacterium Tuberculosis

PAD2 Activity Monitored via a Fluorescent Substrate Analog

2015 ◽  
Vol 86 (4) ◽  
pp. 599-605
Author(s):  
Mary J. Sabulski ◽  
Yanming Wang ◽  
Marcos M. Pires
Keyword(s):  
Fluorescent Substrate ◽  
Substrate Analog

scholarly journals Translation and folding of single proteins in real time

2017 ◽  
Vol 114 (22) ◽  
pp. E4399-E4407 ◽  
Author(s):  
Florian Wruck ◽  
Alexandros Katranidis ◽  
Knud H. Nierhaus ◽  
Georg Büldt ◽  
Martin Hegner
Keyword(s):  
Protein Folding ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Real Time ◽  
Electrostatic Interactions ◽  
Tertiary Structure ◽  
Chain Elongation ◽  
Ribosomal Tunnel ◽  
Cotranslational Folding ◽  
Nascent Chain

Protein biosynthesis is inherently coupled to cotranslational protein folding. Folding of the nascent chain already occurs during synthesis and is mediated by spatial constraints imposed by the ribosomal exit tunnel as well as self-interactions. The polypeptide’s vectorial emergence from the ribosomal tunnel establishes the possible folding pathways leading to its native tertiary structure. How cotranslational protein folding and the rate of synthesis are linked to a protein’s amino acid sequence is still not well defined. Here, we follow synthesis by individual ribosomes using dual-trap optical tweezers and observe simultaneous folding of the nascent polypeptide chain in real time. We show that observed stalling during translation correlates with slowed peptide bond formation at successive proline sequence positions and electrostatic interactions between positively charged amino acids and the ribosomal tunnel. We also determine possible cotranslational folding sites initiated by hydrophobic collapse for an unstructured and two globular proteins while directly measuring initial cotranslational folding forces. Our study elucidates the intricate relationship among a protein’s amino acid sequence, its cotranslational nascent-chain elongation rate, and folding.

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