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Abstract
N-α-terminal acetylation is one of the most common, but least understood modifications of eukaryotic proteins. Although a high degree of conservation exists between the N-α-terminal acetylomes of plants and animals, very little information is available on this modification in plants. In yeast and humans, N-α-acetyltransferase complexes include a single catalytic subunit and one or two auxiliary subunits. Here, we report the positional cloning of TRANSCURVATA2 (TCU2), which encodes the auxiliary subunit of the NatB N-α-acetyltransferase complex in Arabidopsis. The phenotypes of loss-of-function tcu2 alleles indicate that NatB complex activity is required for flowering time regulation and for leaf, inflorescence, flower, fruit and embryonic development. In double mutants, tcu2 alleles synergistically interact with alleles of ARGONAUTE10, which encodes a component of the microRNA machinery. In summary, NatB-mediated N-α-terminal acetylation of proteins is pleiotropically required for Arabidopsis development and seems to be functionally related to the microRNA pathway.
Highlights
One of the most common modifications of eukaryotic proteins is N-a-acetylation of the amino terminus, which is found in 50–70% of yeast proteins and 70–90% of human proteins, but occurs only rarely in prokaryotic proteins
We developed new molecular markers (Table S1), most of them based on the small insertions or deletions (In/Del) described in the Monsanto database and used them for the analysis of a mapping population of 1,137 F2 plants derived from a P14 6.36Col-0 cross
Many eukaryotic proteins are subjected to N-aterminal acetylation, the function of this co- and post-translational modification is known only for a few proteins in a few species, Homo sapiens and Saccharomyces cerevisiae in particular
Summary
One of the most common modifications of eukaryotic proteins is N-a-acetylation of the amino terminus, which is found in 50–70% of yeast proteins and 70–90% of human proteins, but occurs only rarely in prokaryotic proteins (reviewed in [1]). N-a-terminal acetylation involves several complexes, termed NatA to NatF, which exhibit substrate specificity (reviewed in [1]). The Nat (N-acetyltransferase 3) and Mdm (mitochondrial morphology and distribution 20) subunits of the yeast and human NatB complex cosediment with ribosomes, which suggests that they act on nascent polypeptides [3,4,5]. The Ard (Naa10) catalytic subunit of the human NatA complex has been isolated in cytoplasmic and nuclear fractions, which suggests additional functions for Ard, other than cotranslational N-a-terminal acetylation [7]. Recent work showed that the X-linked Ogden syndrome is caused by a specific missense mutation affecting the Naa catalytic subunit of the human NatA complex [8]
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