INT182413
From wiki-pain
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Sentences Mentioned In
Key: | Protein | Mutation | Event | Anatomy | Negation | Speculation | Pain term | Disease term |
Interestingly, the anti-phosphoserine recognized a phosphorylated form of the enzyme in both EGFP-hOGG1 and EGFP-hOGG1-Glu326 chromatin fractions.
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We have previously shown that hOGG1 is associated with the soluble chromatin and the nuclear matrix during interphase and with condensed chromatin during mitosis (47). | |||||||||||||||
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As EGFP-hOGG1 has been shown to be associated with the soluble chromatin and the nuclear matrix during interphase (47), we wanted to investigate whether these associations were maintained for the EGFP-hOGG1-Cys326 mutant protein. | |||||||||||||||
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By sequentially extracting the cells to obtain cytoplasm, soluble chromatin and the nuclear matrix, we were able to show that EGFP-hOGG1-Glu326 was associated with both the soluble chromatin and the nuclear matrix fractions (Figure 7D, lanes 2 and 4). | |||||||||||||||
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Within the next 2 h, cells enter the M-phase, the nuclear envelope disassembles and EGFP-hOGG1 associates with chromatin (Figure 4). | |||||||||||||||
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The pEYFP-hOGG1 plasmid was constructed by ligating the hOGG1 cDNA fragment from pEGFP-hOGG1 into the pEYFP-N1 vector. | |||||||||||||||
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As neither a functional nor a physical direct interaction was detected between these two proteins, the authors hypothesize a protein complex containing among others CSB and hOGG1. | |||||||||||||||
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The pEYFP-hOGG1 plasmid was constructed by ligating the hOGG1 cDNA fragment from pEGFP-hOGG1 into the pEYFP-N1 vector. | |||||||||||||||
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As shown in Figure 2B, EGFP-hOGG1 is associated with the nucleoli during S-phase. | |||||||||||||||
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Interestingly, the anti-phosphoserine recognized a phosphorylated form of the enzyme in both EGFP-hOGG1 and EGFP-hOGG1-Glu326 chromatin fractions.
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Thus, the nucleolus might be a sequestering compartment of hOGG1 to avoid the accumulation of GC? | |||||||||||||||
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Finally, we wanted to examine whether EGFP-hOGG1-Glu326 would also be associated with the soluble chromatin and the nuclear matrix. | |||||||||||||||
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Finally, by mimicking a hOGG1 protein phosphorylated at Ser-326 we demonstrate that the regulation of the nucleolar localization, soluble chromatin, nuclear matrix and condensed chromatin association of hOGG1 are mediated through the phosphorylation of Ser-326.
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EGFP (30 kDa), EGFP-hOGG1, EGFP-hOGG1-Cys326 and EGFP-hOGG1-Glu326 (68 kDa) were recognized by the anti-GFP specific antibody (Figure 3A) while only EGFP-hOGG1, EGFP-hOGG1-Cys326 and EGFP-hOGG1-Glu326 (68 kDa) were recognized by the anti-OGG1 specific antibody (Figure 3B). | |||||||||||||||
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Thus, compartmentalization of hOGG1 to the nucleoli during S-phase might increase the repair efficiency of A:8-oxoG mispairs that arise during DNA replication, as dCMP or dAMP can be selectively incorporated opposite 8-oxoG (7). | |||||||||||||||
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Thus, we suggest that the Ser-326 has to be phosphorylated to interact with a protein during S-phase that will translocate EGFP-hOGG1 to the nucleolus and to the condensed chromosomes during mitosis. | |||||||||||||||
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In humans, 8-oxodG is repaired by 8-oxoguanine DNA glycosylase (OGG1), an enzyme that recognizes and hydrolyzes the aberrant base from the DNA backbone. | |||||||||||||||
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OGG1 is the DNA repair enzyme that recognizes and excises 8-oxodG [70]. | |||||||||||||||
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In humans, 8-oxodG is repaired by 8-oxoguanine DNA glycosylase (OGG1), an enzyme that recognizes and hydrolyzes the aberrant base from the DNA backbone. | |||||||||||||||
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They identified showed the presence of significant association between the Ser326Cys polymorphism of OGG1 and AML. | |||||||||||||||
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