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1                                              NatA co-translationally acetylates the N termini of a wi
2 rprisingly, this enzyme is able to acetylate NatA and NatE substrates and is believed to represent an
3             The N-terminal acetyltransferase NatA is a heterodimeric complex consisting of a catalyti
4 , and the three N(alpha)-acetyltransferases, NatA, NatB, and NatC, which collectively modify approxim
5 pes of N(alpha)-terminal acetyltransferases, NatA, NatB, and NatC, with each having a different catal
6 ases significantly after drought stress, and NatA abundance is rapidly downregulated by the phytohorm
7 t each other's NAT activity in vitro Because NatA and Naa50 exhibit distinct substrate specificity, w
8 tress and that imprinting of the proteome by NatA is an important switch for the control of metabolis
9 N-terminal acetyl transferases (NATs), i.e., NatA, NatB, and NatC, which require as few as two specif
10  molecular dynamics simulations of the human NatA and its S37P mutant highlight differences in region
11 +)] phenotype is reversed in strains lacking NatA.
12 f three N-terminal acetyltransferases (NAT), NatA, NatB, and NatC, which contain Ard1p, Nat3p and Mak
13                To date, two eukaryotic NATs, NatA and NatE, have been structurally characterized, of
14 the Arg/N-end rule pathway in the absence of NatA, and showed that a number of Hsp90 clients are prev
15 plex and reveal evolutionary conservation of NatA biochemical properties in higher eukaryotes and unc
16                  Strikingly, co-depletion of NatA, a heterodimeric NAT complex that physically intera
17    Accordingly, transgenic downregulation of NatA induces the drought stress response and results in
18  uncover specific and essential functions of NatA for development, biosynthetic pathways and stress r
19 ealed a decreased acetylation of a subset of NatA and NatE substrates in Ogden syndrome cells, suppor
20 arding reduced Nt-acetylation of a subset of NatA/NatE-type substrates as one etiology for Ogden synd
21 ene encoding Naa10, the catalytic subunit of NatA, the major human NAT involved in the co-translation
22               Here we characterize the plant NatA complex and reveal evolutionary conservation of Nat
23   Despite this change in phenotype, [PSI(+)] NatA mutants continue to propagate heritable Sup35([PSI+
24                                      Rather, NatA null strains are specifically impaired in establish
25                         Purified recombinant NatA and Naa50 do not affect each other's NAT activity i
26 t caused by Naa50 depletion, indicating that NatA and Naa50 play antagonistic roles in cohesion.
27                                          The NatA effect cannot be explained by the modification of k
28         Sir3 and, perhaps, also Orc1 are the NatA substrates whose lack of acetylation in ard1 and na
29             Thus, we propose that NTA by the NatA complex acts as a cellular surveillance mechanism d
30 otein Sir3 and of Orc1 are acetylated by the NatA Nalpha-acetyltransferase.
31 equired for N-terminal acetylation, i.e. the NatA, NatB, and NatC substrates, were evaluated by consi
32 impaired in naa10Delta cells, which lack the NatA N(alpha)-terminal acetylase (Nt-acetylase) and ther
33 iates with the Nat1 and Ard1 subunits of the NatA acetyltransferase.
34 ive site of ssNAT represents a hybrid of the NatA and NatE active sites, and we highlight features of
35 l as Naa50 (NatE), another interactor of the NatA complex.
36 ld be overridden not only by ablation of the NatA Nt-acetylase but also by overexpression of the Arg/
37 h a small fraction of San interacts with the NatA complex, San appears to mediate cohesion independen
38 minal-acetylated, and 24 of these (80%) were NatA substrates, unacetylated in solely the ard1-Delta m
39 ve been structurally characterized, of which NatA will acetylate the alpha-amino group of a number of

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