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2014 ; 11
(8
): 1072-82
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Structural analyses of the CRISPR protein Csc2 reveal the RNA-binding interface
of the type I-D Cas7 family
#MMPMID25483036
Hrle A
; Maier LK
; Sharma K
; Ebert J
; Basquin C
; Urlaub H
; Marchfelder A
; Conti E
RNA Biol
2014[]; 11
(8
): 1072-82
PMID25483036
show ga
Upon pathogen invasion, bacteria and archaea activate an RNA-interference-like
mechanism termed CRISPR (clustered regularly interspaced short palindromic
repeats). A large family of Cas (CRISPR-associated) proteins mediates the
different stages of this sophisticated immune response. Bioinformatic studies
have classified the Cas proteins into families, according to their sequences and
respective functions. These range from the insertion of the foreign genetic
elements into the host genome to the activation of the interference machinery as
well as target degradation upon attack. Cas7 family proteins are central to the
type I and type III interference machineries as they constitute the backbone of
the large interference complexes. Here we report the crystal structure of
Thermofilum pendens Csc2, a Cas7 family protein of type I-D. We found that Csc2
forms a core RRM-like domain, flanked by three peripheral insertion domains: a
lid domain, a Zinc-binding domain and a helical domain. Comparison with other
Cas7 family proteins reveals a set of similar structural features both in the
core and in the peripheral domains, despite the absence of significant sequence
similarity. T. pendens Csc2 binds single-stranded RNA in vitro in a
sequence-independent manner. Using a crosslinking - mass-spectrometry approach,
we mapped the RNA-binding surface to a positively charged surface patch on T.
pendens Csc2. Thus our analysis of the key structural and functional features of
T. pendens Csc2 highlights recurring themes and evolutionary relationships in
type I and type III Cas proteins.
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