Changes in Targeting Efficiencies of Proteins to Plant Microbodies Caused by Amino Acid Substitutions in the Carboxy-terminal Tripeptide
Open Access
- 1 January 1997
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant and Cell Physiology
- Vol. 38 (6) , 759-768
- https://doi.org/10.1093/oxfordjournals.pcp.a029233
Abstract
It has been demonstrated that the carboxyl terminus of microbody enzymes functions as a targeting signal to microbodies in higher plants. We have examined an ability of 24 carboxy-terminal amino acid sequences to facilitate the transport of a cytosolic passenger protein, β-glucuroni-dase, into microbodies in green cotyledonary cells of trans-genic Arabidopsis. Immunoelectron microscopic analysis revealed that carboxy-terminal tripeptide sequences of the form [C/A/S/P]-[K/R]-[I/L/M] function as a microbody-targeting signal, although tripeptides with proline at the first amino acid position and isoleucine at the carboxyl terminus show weak targeting efficiencies. All known micro-body enzymes that are synthesized in a form similar in size to the mature molecule, except catalase, contain one of these tripeptide sequences at their carboxyl terminus.Keywords
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