TY  - JOUR
A1  - Grimm, Clemens
A1  - Pelz, Jann-Patrick
A1  - Schneider, Cornelius
A1  - Schäffler, Katrin
A1  - Fischer, Utz
T1  - Crystal Structure of a Variant PAM2 Motif of LARP4B Bound to the MLLE Domain of PABPC1
JF  - Biomolecules
N2  - Eukaryotic cells determine the protein output of their genetic program by regulating mRNA transcription, localization, translation and turnover rates. This regulation is accomplished by an ensemble of RNA-binding proteins (RBPs) that bind to any given mRNA, thus forming mRNPs. Poly(A) binding proteins (PABPs) are prominent members of virtually all mRNPs that possess poly(A) tails. They serve as multifunctional scaffolds, allowing the recruitment of diverse factors containing a poly(A)-interacting motif (PAM) into mRNPs. We present the crystal structure of the variant PAM motif (termed PAM2w) in the N-terminal part of the positive translation factor LARP4B, which binds to the MLLE domain of the poly(A) binding protein C1 cytoplasmic 1 (PABPC1). The structural analysis, along with mutational studies in vitro and in vivo, uncovered a new mode of interaction between PAM2 motifs and MLLE domains.
KW  - PAM2w
KW  - PAM2
KW  - PABC1
KW  - MLLE domain
KW  - PABP
KW  - Poly(A) binding protein
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-207800
SN  - 2218-273X
VL  - 10
IS  - 6
ER  -