 |
PDBsum entry 4xq3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
RNA binding protein
|
PDB id
|
|
|
|
4xq3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The heptameric smap1 and smap2 proteins of the crenarchaeon sulfolobus solfataricus bind to common and distinct RNA targets.
|
|
|
Authors
|
|
B.Märtens,
G.A.Bezerra,
M.J.Kreuter,
I.Grishkovskaya,
A.Manica,
V.Arkhipova,
K.Djinovic-Carugo,
U.Bläsi.
|
|
|
Ref.
|
|
Life (basel), 2015,
5,
1264-1281.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Sm and Sm-like proteins represent an evolutionarily conserved family with key
roles in RNA metabolism. Sm-based regulation is diverse and can range in scope
from eukaryotic mRNA splicing to bacterial quorum sensing, with at least one
step in these processes being mediated by an RNA-associated molecular assembly
built on Sm proteins. Despite the availability of several 3D-structures of
Sm-like archaeal proteins (SmAPs), their function has remained elusive. The aim
of this study was to shed light on the function of SmAP1 and SmAP2 of the
crenarchaeon Sulfolobus solfataricus (Sso). Using co-purification followed by
RNASeq different classes of non-coding RNAs and mRNAs were identified that
co-purified either with both paralogues or solely with Sso-SmAP1 or Sso-SmAP2.
The large number of associated intron-containing tRNAs and tRNA/rRNA modifying
RNAs may suggest a role of the two Sso-SmAPs in tRNA/rRNA processing. Moreover,
the 3D structure of Sso-SmAP2 was elucidated. Like Sso-SmAP1, Sso-SmAP2 forms
homoheptamers. The binding of both proteins to distinct RNA substrates is
discussed in terms of surface conservation, structural differences in the RNA
binding sites and differences in the electrostatic surface potential of the two
Sso-SmAP proteins. Taken together, this study may hint to common and different
functions of both Sso-SmAPs in Sso RNA metabolism.
|
|
|
|
|
|
|
