Evidence for an inhibitory LIM domain in a rat brain agmatinase-like protein.

Abstract:

:We recently cloned a rat brain agmatinase-like protein (ALP) whose amino acid sequence greatly differs from other agmatinases and exhibits a LIM-like domain close to its carboxyl terminus. The protein was immunohistochemically detected in the hypothalamic region and hippocampal astrocytes and neurons. We now show that truncated species, lacking the LIM-type domain, retains the dimeric structure of the wild-type protein but exhibits a 10-fold increased k(cat), a 3-fold decreased K(m) value for agmatine and altered intrinsic tryptophan fluorescent properties. As expected for a LIM protein, zinc was detected only in the wild-type ALP (∼2 Zn(2+)/monomer). Our proposal is that the LIM domain functions as an autoinhibitory entity and that inhibition is reversed by interaction of the domain with some yet undefined brain protein.

journal_name

Arch Biochem Biophys

authors

Castro V,Fuentealba P,Henríquez A,Vallejos A,Benítez J,Lobos M,Díaz B,Carvajal N,Uribe E

doi

10.1016/j.abb.2011.05.003

subject

Has Abstract

pub_date

2011-08-01 00:00:00

pages

107-10

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(11)00175-5

journal_volume

512

pub_type

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