scholarly journals Cytoplasmic N-Terminal Protein Acetylation Is Required for Efficient Photosynthesis in Arabidopsis

2003 ◽  
Vol 15 (8) ◽  
pp. 1817-1832 ◽  
Author(s):  
Paolo Pesaresi ◽  
Nora A. Gardner ◽  
Simona Masiero ◽  
Angela Dietzmann ◽  
Lutz Eichacker ◽  
...  
2018 ◽  
Vol 293 (8) ◽  
pp. 2927-2938 ◽  
Author(s):  
Trevor Croft ◽  
Christol James Theoga Raj ◽  
Michelle Salemi ◽  
Brett S. Phinney ◽  
Su-Ju Lin

BioEssays ◽  
2019 ◽  
Vol 41 (11) ◽  
pp. 1800167 ◽  
Author(s):  
Mohamed A. Eldeeb ◽  
Richard P. Fahlman ◽  
Mohamed A. Ragheb ◽  
Mansoore Esmaili

2019 ◽  
Author(s):  
Trevor Croft ◽  
Padmaja Venkatakrishnan ◽  
Christol James Theoga Raj ◽  
Benjamin Groth ◽  
Timothy Cater ◽  
...  

ABSTRACTNAD+ is an essential metabolite participating in cellular biochemical processes and signaling. The regulation and interconnection among multiple NAD+ biosynthesis pathways are not completely understood. We previously identified the N-terminal (Nt) protein acetyltransferase complex NatB as a NAD+ homeostasis factor. Cells lacking NatB show an approximate 50% reduction in the NAD+ level and aberrant metabolism of NAD+ precursors, which are associated with a decrease of nicotinamide mononucleotide adenylyltransferases (Nmnat) protein levels. Here we show this decrease in NAD+ and Nmnat protein levels is specifically due to the absence of Nt-acetylation of Nmnat (Nma1 and Nma2) proteins, and not other NatB substrates. Nt-acetylation is a critical regulator of protein degradation by the N-end rule pathways, indicating absence of Nt-acetylation may alter Nmnat protein stability. Interestingly, the rate of protein turnover (t1/2) of non-Nt-acetylated Nmnats does not significantly differ from Nt-acetylated Nmnats, suggesting reduced Nmnat levels in NmatB mutants are not due to increased post-translational degradation of non-Nt-acetylated Nmnats. In line with these observations, deletion or depletion of N-rule pathway ubiquitin E3 ligases in NatB mutants is not sufficient to restore NAD+ levels. Moreover, the status of Nt-acetylation does not alter the rate of translation initiation of Nmnats. Collectively our studies suggest absence of Nt-acetylation may increase co-translational degradation of nascent Nmnat polypeptides, which results in reduced Nmnat levels in NatB mutants. Nmnat activities are essential for all routes of NAD+ biosynthesis. Understanding the regulation of Nmnat protein homeostasis will facilitate our understanding of the molecular basis and regulation of NAD+ metabolism.


2012 ◽  
Vol 393 (4) ◽  
pp. 291-298 ◽  
Author(s):  
Jolien Hollebeke ◽  
Petra Van Damme ◽  
Kris Gevaert

Abstract Protein N-terminal acetylation by Nα-acetyltransferases (NATs) is an omnipresent protein modification that affects a large number of proteins. The exact biological role of N-terminal acetylation has, however, remained enigmatic for the overall majority of affected proteins, and only for a rather small number of proteins, N-terminal acetylation was linked to various protein features including stability, localization, and interactions. This minireview tries to summarize the recent progress made in understanding the functionality of N-terminal protein acetylation and also focuses on noncanonical functions of the NATs subunits.


Author(s):  
Yuexia Liu ◽  
Hong Yang ◽  
Xuanchen Liu ◽  
Huihui Gu ◽  
Yizhou Li ◽  
...  
Keyword(s):  

Sign in / Sign up

Export Citation Format

Share Document