High impact information on MMS19L

• In contrast, over expression of the full-length hMMS19 enhances ER-mediated transcriptional activation [1].
• In contrast, a VEGF121 variant covering amino acids 18 to 121, as well as a variant in which the hydrophobic amino acids Val14, Val15, Phe17, and Met18 within the amphipathic alpha-helix near the amino terminus were replaced by serine, failed to form biological active VEGF dimers [2].
• The relationship between the conformational properties of 1-34 human parathyroid hormone [hPTH(1-34)] and the oxidation of its methionine residues, Met8 and Met18, by hydrogen peroxide is analyzed as a function of pH by measuring the rates of oxidation and by performing MD simulations with an explicit representation of water molecules [3].
• Asn9, Met18, and Ser87 residues were modified by site-directed mutagenesis to probe the function of the interface residues in porcine liver fructose-1,6-bisphosphatase [4].
• RESULTS: Three oxidized products were isolated, namely, Met at position 8 (Met8) sulfoxide, Met at position 18 (Met18) sulfoxide and both positions Met sulfoxide [5].

Biological context of MMS19L

• Our data suggest that the MMS19 HEAT repeat domain is essential for MMS19 function in NER and transcription, while domains A and B, within MMS19 N-terminus, modulate the balance between DNA repair and transcription [6].

Other interactions of MMS19L

• These findings extend the conservation of the NER apparatus and the link between NER and basal transcription and suggest that hMMS19 exerts its function in repair and transcription by interacting with the XPB and XPD helicases [7].
• Expression of human MMS19 splice variants in mms19-deleted yeast cells produced unique patterns of thermosensitivity and ultraviolet radiation-sensitivity that point to three MMS19 structural domains with distinct in vivo functions [6].
• Like TFIIH, MMS19 is required for NER and Pol II transcription, but its precise role in each process is unknown [6].

Analytical, diagnostic and therapeutic context of MMS19L

• Complete oxidation of Met3, Met18 and Met55 was observed after treatment with H2O2, while these residues underwent 40 to 60% oxidation after treatment with t-BHP [8].

References