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Comparative analysis of cone and rod transducins using chimeric G? subunits.


ABSTRACT: The molecular nature of transducin-? subunits (G?(t)) may contribute to the distinct physiology of cone and rod photoreceptors. Biochemical properties of mammalian cone G?(t2) subunits and their differences with rod G?(t1) are largely unknown. Here, we examined properties of chimeric G?(t2) in comparison with its rod counterpart. The key biochemical difference between the rod- and cone-like G?(t) was ~10-fold higher intrinsic nucleotide exchange on the chimeric G?(t2). Presented mutational analysis suggests that weaker interdomain interactions between the GTPase (Ras-like) domain and the helical domain in G?(t2) are in part responsible for its increased spontaneous nucleotide exchange. However, the rates of R*-dependent nucleotide exchange of chimeric G?(t2) and G?(t1) were equivalent. Furthermore, chimeric G?(t2) and G?(t1) exhibited similar rates of intrinsic GTPase activity as well as similar acceleration of GTP hydrolysis by the RGS domain of RGS9. Our results suggest that the activation and inactivation properties of cone and rod G?(t) subunits in an in vitro reconstituted system are comparable.

SUBMITTER: Gopalakrishna KN 

PROVIDER: S-EPMC3291952 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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Comparative analysis of cone and rod transducins using chimeric Gα subunits.

Gopalakrishna Kota N KN   Boyd Kimberly K KK   Artemyev Nikolai O NO  

Biochemistry 20120216 8


The molecular nature of transducin-α subunits (Gα(t)) may contribute to the distinct physiology of cone and rod photoreceptors. Biochemical properties of mammalian cone Gα(t2) subunits and their differences with rod Gα(t1) are largely unknown. Here, we examined properties of chimeric Gα(t2) in comparison with its rod counterpart. The key biochemical difference between the rod- and cone-like Gα(t) was ~10-fold higher intrinsic nucleotide exchange on the chimeric Gα(t2). Presented mutational analy  ...[more]

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