Abstract
Ribosome biogenesis is one of the most energy demanding processes in the cell. In eukaryotes, the main steps of this process occur in the nucleolus and include pre-ribosomal RNA (pre-rRNA) processing, post-transcriptional modifications, and assembly of many non-ribosomal factors and ribosomal proteins in order to form mature and functional ribosomes. In yeast and humans, the nucleolar RNA acetyltransferase Kre33/NAT10 participates in different maturation events, such as acetylation and processing of 18S rRNA, and assembly of the 40S ribosomal subunit. Here, we review the structural and functional features of Kre33/NAT10 RNA acetyltransferase, and we underscore the importance of this enzyme in ribosome biogenesis, as well as in acetylation of non-ribosomal targets. We also report on the role of human NAT10 in Hutchinson–Gilford progeria syndrome.
Highlights
Mutations in the DNA sequence of the genome can be caused by many factors, including errors in DNA replication or failure of the DNA repair system of the cell, and can lead to various changes at the protein level, such as altering their expression, folding, function and stability [1]
In the past few years, cryo-electron microscopy (EM) structures of the S. cerevisiae small subunit (SSU) processome have been reported, revealing that Kre33 acetyltransferase forms a dimer in the SSU processome and connects Bms1 guanosine triphosphate hydroxylase (GTPase) and Enp2 [66,68,73,132]
The coiled-coil motif in the CTE of Kre33 may be responsible for protein–protein interaction, but the current available structures of Kre33 in the SSU processome do not allow us to determine the position of the C-terminal extension, precluding the identification of the sites of interaction
Summary
Mutations in the DNA sequence of the genome can be caused by many factors, including errors in DNA replication or failure of the DNA repair system of the cell, and can lead to various changes at the protein level, such as altering their expression, folding, function and stability [1]. The making of ribosomes begins within the nucleolus, continues in the nucleoplasm and terminates in the cytoplasm [10,11] This process involves ribosomal RNA (rRNA) transcription, processing, modification and assembly reactions that are finely tuned and lead to the formation of two large ribonucleoprotein (RNP) complexes: the small and large ribosomal subunits (40S and 60S, respectively) [12]. Ribosome biogenesis implicates more than 200 non-ribosomal factors, and a large number of these proteins are part of the small subunit (SSU) processome complex. This highly dynamic RNP of 80S–90S is essential for assembly of the 40S subunit, and consists of the. A small daughter cell grows from a large mother cell and conveys its own transcription program; the nucleus is round during interphase and adopts an hourglass shape during mitosis [29,30]
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