title: 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.
authors: Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción, Chile.
authors: Víctor
authors: V
authors: Castro
authors: Pablo
authors: P
authors: Fuentealba
authors: Adolfo
authors: A
authors: Henríquez
authors: Alejandro
authors: A
authors: Vallejos
authors: José
authors: J
authors: Benítez
authors: Marcela
authors: M
authors: Lobos
authors: Beatriz
authors: B
authors: Díaz
authors: Nelson
authors: N
authors: Carvajal
authors: Elena
authors: E
authors: Uribe