scholarly journals Structural and functional characterization of the rod outer segment membrane guanylate cyclase

1994 ◽  
Vol 302 (2) ◽  
pp. 455-461 ◽  
Author(s):  
R M Goraczniak ◽  
T Duda ◽  
A Sitaramayya ◽  
R K Sharma
Keyword(s):  
Cyclic Gmp ◽  
Outer Segment ◽  
Photoreceptor Cell ◽  
Functional Characterization ◽  
Visual Signal ◽  
Membrane Guanylate Cyclase ◽  
Rod Outer Segment ◽  
Vertebrate Photoreceptor ◽  
Hydrolysis Of

In the vertebrate photoreceptor cell, rod outer segment (ROS) is the site of visual signal-transduction process, and a pivotal molecule that regulates this process is cyclic GMP. Cyclic GMP controls the cationic conductance into the ROS, and light causes a decrease in the conductance by activating hydrolysis of the cyclic nucleotide. The identity of the granylate cyclase (ROS-GC) that synthesizes this pool of cyclic GMP is unknown. We now report the cloning, expression and functional characterization of a DNA from bovine retina that encodes ROS-GC.

Rod outer segment phosphodiesterase: Factors affecting the hydrolysis of cyclic-AMP and cyclic-GMP

1974 ◽  
Vol 18 (6) ◽  
pp. 509-515 ◽  
Author(s):  
G. Chader ◽  
R. Fletcher ◽  
M. Johnson ◽  
R. Bensinger
Keyword(s):  
Cyclic Amp ◽  
Cyclic Gmp ◽  
Outer Segment ◽  
Factors Affecting ◽  
Rod Outer Segment ◽  
Hydrolysis Of

scholarly journals Impairment of the Rod Outer Segment Membrane Guanylate Cyclase Dimerization in A Cone−Rod Dystrophy Results in Defective Calcium Signaling†

Biochemistry ◽  
2000 ◽  
Vol 39 (41) ◽  
pp. 12522-12533 ◽  
Author(s):  
Teresa Duda ◽  
Venkateswar Venkataraman ◽  
Anna Jankowska ◽  
Christian Lange ◽  
Karl-W. Koch ◽  
...  
Keyword(s):  
Calcium Signaling ◽  
Guanylate Cyclase ◽  
Outer Segment ◽  
Membrane Guanylate Cyclase ◽  
Rod Outer Segment

scholarly journals Calcium-Modulated Rod Outer Segment Membrane Guanylate Cyclase Type 1 Transduction Machinery in the Testes

2006 ◽  
Vol 28 (1) ◽  
pp. 50-58 ◽  
Author(s):  
A. Jankowska ◽  
B. Burczynska ◽  
T. Duda ◽  
J. B. Warchol ◽  
R. K. Sharma
Keyword(s):  
Guanylate Cyclase ◽  
Outer Segment ◽  
Membrane Guanylate Cyclase ◽  
Rod Outer Segment

scholarly journals Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain

2005 ◽  
Vol 388 (2) ◽  
pp. 493-500 ◽  
Author(s):  
Chandra N. PATEL ◽  
David W. KOH ◽  
Myron K. JACOBSON ◽  
Marcos A. OLIVEIRA
Keyword(s):  
Catalytic Activity ◽  
Catalytic Domain ◽  
Functional Characterization ◽  
Sequence Alignments ◽  
Inhibitor Binding ◽  
Conserved Sequence ◽  
Binding Residue ◽  
Acidic Residues ◽  
Hydrolysis Of

PARG [poly(ADP-ribose) glycohydrolase] catalyses the hydrolysis of α(1″→2′) or α(1‴→2″) O-glycosidic linkages of ADP-ribose polymers to produce free ADP-ribose. We investigated possible mechanistic similarities between PARG and glycosidases, which also cleave O-glycosidic linkages. Glycosidases typically utilize two acidic residues for catalysis, thus we targeted acidic residues within a conserved region of bovine PARG that has been shown to contain an inhibitor-binding site. The targeted glutamate and aspartate residues were changed to asparagine in order to minimize structural alterations. Mutants were purified and assayed for catalytic activity, as well as binding, to an immobilized PARG inhibitor to determine ability to recognize substrate. Our investigation revealed residues essential for PARG catalytic activity. Two adjacent glutamic acid residues are found in the conserved sequence Gln755-Glu-Glu757, and a third residue found in the conserved sequence Val737-Asp-Phe-Ala-Asn741. Our functional characterization of PARG residues, along with recent identification of an inhibitor-binding residue Tyr796 and a glycine-rich region Gly745-Gly-Gly747 important for PARG function, allowed us to define a PARG ‘signature sequence’ [vDFA-X3-GGg-X6–8-vQEEIRF-X3-PE-X14-E-X12-YTGYa], which we used to identify putative PARG sequences across a range of organisms. Sequence alignments, along with our mapping of PARG functional residues, suggest the presence of a conserved catalytic domain of approx. 185 residues which spans residues 610–795 in bovine PARG.

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