Fragile X mental retardation protein recognition of G quadruplex structure per se is sufficient for high affinity binding to RNA

2008 ◽  
Vol 4 (12) ◽  
pp. 1212 ◽  
Author(s):  
Medhavi Bole ◽  
Lakshmi Menon ◽  
Mihaela-Rita Mihailescu
Keyword(s):  
Fragile X ◽  
Protein Recognition ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
Fragile X Mental Retardation ◽  
High Affinity ◽  
Quadruplex Structure ◽  
G Quadruplex ◽  
Mental Retardation Protein ◽  
Per Se

scholarly journals Fragile X mental retardation protein interactions with a G quadruplex structure in the 3′-untranslated region of NR2B mRNA

2015 ◽  
Vol 11 (12) ◽  
pp. 3222-3230 ◽  
Author(s):  
Snezana Stefanovic ◽  
Brett A. DeMarco ◽  
Ayana Underwood ◽  
Kathryn R. Williams ◽  
Gary J. Bassell ◽  
...  
Keyword(s):  
Mental Retardation ◽  
Intellectual Disability ◽  
Protein Interactions ◽  
Untranslated Region ◽  
Fragile X ◽  
Common Cause ◽  
Fragile X Mental Retardation ◽  
Quadruplex Structure ◽  
G Quadruplex ◽  
Mental Retardation Protein

Fragile X syndrome, the most common cause of inherited intellectual disability, is caused by a trinucleotide CGG expansion in the 5′-untranslated region of the FMR1 gene, which leads to the loss of expression of the fragile X mental retardation protein (FMRP).

scholarly journals Fragile X mental retardation protein recognizes a G quadruplex structure within the survival motor neuron domain containing 1 mRNA 5′-UTR

2017 ◽  
Vol 13 (8) ◽  
pp. 1448-1457 ◽  
Author(s):  
Damian S. McAninch ◽  
Ashley M. Heinaman ◽  
Cara N. Lang ◽  
Kathryn R. Moss ◽  
Gary J. Bassell ◽  
...  
Keyword(s):  
Mental Retardation ◽  
Motor Neuron ◽  
Fragile X ◽  
Survival Motor Neuron ◽  
Spliceosome Assembly ◽  
Fragile X Mental Retardation ◽  
Quadruplex Structure ◽  
G Quadruplex ◽  
Mental Retardation Protein

SMNDC1 mRNA adopts a 5′-UTR G quadruplex structure recognized specifically by FMRP, potentially affecting spliceosome assembly in FXS.

Specific High-Affinity Binding of Thiazole Orange to Triplex and G-Quadruplex DNA

Biochemistry ◽  
2010 ◽  
Vol 49 (17) ◽  
pp. 3567-3574 ◽  
Author(s):  
Irit Lubitz ◽  
Dragoslav Zikich ◽  
Alexander Kotlyar
Keyword(s):  
Affinity Binding ◽  
Thiazole Orange ◽  
High Affinity Binding ◽  
Quadruplex Dna ◽  
High Affinity ◽  
G Quadruplex

Characterization of a Mode of Specific Binding of Fibrin Monomer through its Amino-Terminal Domain by Macrophages and Macrophage Cell-Lines

1990 ◽  
Vol 63 (02) ◽  
pp. 193-203 ◽  
Author(s):  
John R Shainoff ◽  
Deborah J Stearns ◽  
Patricia M DiBello ◽  
Youko Hishikawa-Itoh
Keyword(s):  
Peritoneal Macrophages ◽  
Affinity Binding ◽  
Macrophage Cell ◽  
High Affinity Binding ◽  
Amino Terminal ◽  
High Affinity ◽  
Terminal Domain ◽  
Weak Binding ◽  
Amino Terminal Domain

SummaryThe studies reported here probe the existence of a receptor-mediated mode of fibrin-binding by macrophages that is associated with the chemical change underlying the fibrinogen-fibrin conversion (the release of fibrinopeptides from the amino-terminal domain) without depending on fibrin-aggregation. The question is pursued by 1) characterization of binding in relation to fibrinopeptide content of both the intact protein and the CNBr-fragment comprising the amino-terminal domain known as the NDSK of the protein, 2) tests of competition for binding sites, and 3) photo-affinity labeling of macrophage surface proteins. The binding of intact monomers of types lacking either fibrinopeptide A alone (α-fibrin) or both fibrinopeptides A and B (αβ-fibrin) by peritoneal macrophages is characterized as proceeding through both a fibrin-specific low density/high affinity (BMAX ≃ 200–800 molecules/cell, KD ≃ 10−12 M) interaction that is not duplicated with fibrinogen, and a non-specific high density/low affinity (BMAX ≥ 105 molecules/cell, KD ≥ 10−6 M) interaction equivalent to the weak binding of fibrinogen. Similar binding characteristics are displayed by monocyte/macrophage cell lines (J774A.1 and U937) as well as peritoneal macrophages towards the NDSK preparations of these proteins, except for a slightly weaker (KD ≃ 10−10 M) high-affinity binding. The high affinity binding of intact monomer is inhibitable by fibrin-NDSK, but not fibrinogen-NDSK. This binding appears principally dependent on release of fibrinopeptide-A, because a species of fibrin (β-fibrin) lacking fibrinopeptide-B alone undergoes only weak binding similar to that of fibrinogen. Synthetic Gly-Pro-Arg and Gly-His-Arg-Pro corresponding to the N-termini of to the α- and the β-chains of fibrin both inhibit the high affinity binding of the fibrin-NDSKs, and the cell-adhesion peptide Arg-Gly-Asp does not. Photoaffinity-labeling experiments indicate that polypeptides with elec-trophoretically estimated masses of 124 and 187 kDa are the principal membrane components associated with specifically bound fibrin-NDSK. The binding could not be up-regulated with either phorbol myristyl acetate, interferon gamma or ADP, but was abolished by EDTA and by lipopolysaccharide. Because of the low BMAX, it is suggested that the high-affinity mode of binding characterized here would be too limited to function by itself in scavenging much fibrin, but may act cooperatively with other, less limited modes of fibrin binding.

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