Scarcity of λ1 B cells in mice with a single point mutation in Cλ1 is due to a low BCR signal caused by misfolded lambda1 light chain

Volgina, Veronica V.; Sun, Tianhe; Bozek, Grazyna; Martin, Terence E.; Storb, Ursula

doi:10.1016/j.molimm.2006.04.022

Cited by 2 publications

(1 citation statement)

References 35 publications

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“…The introduction of strand-balanced, AID-generated dU in DNA can result from at least three mechanisms. First, a biophysical, movement-related mechanism where negative supercoiling is generated on DNA on the wake of the RNA polymerase, dynamically generating short stretches of quasi-stable ssDNA on both strands 30,31 .…”

Section: Discussionmentioning

confidence: 99%

Genetic loss of the ubiquitin ligase RNF126, an AID interacting partner and modifier, affects strand targeting during somatic hypermutation of antibody genes

Economos

Delker

Stavropoulos

et al. 2018

Preprint

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Activation-induced cytidine deaminase (AID) initiates somatic hypermutation (SHM) and class switch recombination (CSR) in B lymphocytes by catalyzing the introduction of deoxyuracil: deoxyguanine mismatches into the DNA of the transcribed Ig locus. Repair pathways then process these mismatches to produce point mutations in the Ig variable region or double-stranded DNA breaks in the switch region followed by deletional recombination. It has been suggested that post-translational modifications on AID mediate a number of these different decisions, ranging from global targeting (Ig vs the genome), local targeting (variable vs switch region; transcribed vs non-transcribed strand) as well as process-appropriate DNA repair. Here we demonstrate that absence of RNF126, an E3 ligase shown to mono-ubiquitylate AID, results in a specific strand targeting defect in SHM, producing substantial G>C bias; strickingly, loss of RNF126 was also associated with tandem indels within the variable region (JH4 intron) but only a slight increase in the types of chromosomal translocations that are characteristic of deregulated AID. Conversely, these findings suggest that mono-ubiquitination of AID, likely in situ, is necessary for the proper removal of the protein from the non-transcribed strand, thus producing both optimal patterns of SHM and also limiting the number of indels within the target locus.

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Section: Discussionmentioning

confidence: 99%

Genetic loss of the ubiquitin ligase RNF126, an AID interacting partner and modifier, affects strand targeting during somatic hypermutation of antibody genes

Economos

Delker

Stavropoulos

et al. 2018

Preprint

View full text Add to dashboard Cite

show abstract

Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry

Suchanova

Tůma

2008

Microb Cell Fact

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Recent advances in protein mass spectrometry (MS) have enabled determinations of hydrogen deuterium exchange (HDX) in large macromolecular complexes. HDX-MS became a valuable tool to follow protein folding, assembly and aggregation. The methodology has a wide range of applications in biotechnology ranging from quality control for over-expressed proteins and their complexes to screening of potential ligands and inhibitors. This review provides an introduction to protein folding and assembly followed by the principles of HDX and MS detection, and concludes with selected examples of applications that might be of interest to the biotechnology community.

show abstract

Scarcity of λ1 B cells in mice with a single point mutation in Cλ1 is due to a low BCR signal caused by misfolded lambda1 light chain

Cited by 2 publications

References 35 publications

Genetic loss of the ubiquitin ligase RNF126, an AID interacting partner and modifier, affects strand targeting during somatic hypermutation of antibody genes

Genetic loss of the ubiquitin ligase RNF126, an AID interacting partner and modifier, affects strand targeting during somatic hypermutation of antibody genes

Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry

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