Functional characterization of <Emphasis Type="Italic">Arabidopsis thaliana</Emphasis> transthyretin-like protein |
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| Authors: | João Pessoa Zsuzsa Sárkány Frederico Ferreira-da-Silva Sónia Martins Maria R Almeida Jianming Li Ana M Damas |
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| Institution: | 1.IBMC - Instituto de Biologia Molecular e Celular,Universidade do Porto,Portugal;2.ICBAS - Instituto de Ciências Biomédicas de Abel Salazar,Universidade do Porto, Largo Prof,Portugal;3.Department of Molecular, Cellular, and Developmental Biology,University of Michigan,Ann Arbor,USA |
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| Abstract: | Background
Arabidopsis thaliana transthyretin-like (TTL) protein is a potential substrate in the brassinosteroid signalling cascade, having a role that moderates
plant growth. Moreover, sequence homology revealed two sequence domains similar to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
(OHCU) decarboxylase (N-terminal domain) and 5-hydroxyisourate (5-HIU) hydrolase (C-terminal domain). TTL is a member of the
transthyretin-related protein family (TRP), which comprises a number of proteins with sequence homology to transthyretin (TTR)
and the characteristic C-terminal sequence motif Tyr-Arg-Gly-Ser. TRPs are single domain proteins that form tetrameric structures
with 5-HIU hydrolase activity. Experimental evidence is fundamental for knowing if TTL is a tetrameric protein, formed by
the association of the 5-HIU hydrolase domains and, in this case, if the structural arrangement allows for OHCU decarboxylase
activity. This work reports about the biochemical and functional characterization of TTL. |
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