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Cover Feature: Interaction of the N‐Terminal Tandem Domains of hnRNP LL with the BCL2 Promoter i‐Motif DNA Sequence (ChemBioChem 20/2017)
Author(s) -
Lannes Laurie,
Young Phoebe,
Richter Christian,
Morgner Nina,
Schwalbe Harald
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700512
Subject(s) - dna , sequence motif , chemistry , computational biology , transcription (linguistics) , genetics , biology , microbiology and biotechnology , biophysics , linguistics , philosophy
The inside cover picture shows the interaction of the transcription factor hnRNP LL with the BCL2 promoter DNA sequence Py39wt. The single‐stranded DNA sequence Py39wt can adopt different conformations in a pH‐dependent manner. Indeed, slightly acidic pH triggers the formation of a tetraplex folding named the i‐motif (left fly), whereas neutral pH leads to a hairpin folding (right fly). The hnRNP LL protein is organised in four RNA recognition motifs (RRMs). In order to bind to Py39wt efficiently, regardless of the DNA conformation, the protein has to engage both of its N‐terminal domains RRM1 and RRM2, like a Venus flytrap simultaneously snaps shut both lobes of its leaves to catch insects. More information can be found in the full paper by H. Schwalbe et al. on page 2033 in Issue 20, 2017 (DOI: 10.1002/cbic.201700390).