Title |
A novel human NatA Nα-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)
|
---|---|
Published in |
BMC Molecular and Cell Biology, May 2009
|
DOI | 10.1186/1471-2091-10-15 |
Pubmed ID | |
Authors |
Thomas Arnesen, Darina Gromyko, Diane Kagabo, Matthew J Betts, Kristian K Starheim, Jan Erik Varhaug, Dave Anderson, Johan R Lillehaug |
Abstract |
Protein acetylation is among the most common protein modifications. The two major types are post-translational Nepsilon-lysine acetylation catalyzed by KATs (Lysine acetyltransferases, previously named HATs (histone acetyltransferases) and co-translational Nalpha-terminal acetylation catalyzed by NATs (N-terminal acetyltransferases). The major NAT complex in yeast, NatA, is composed of the catalytic subunit Naa10p (N alpha acetyltransferase 10 protein) (Ard1p) and the auxiliary subunit Naa15p (Nat1p). The NatA complex potentially acetylates Ser-, Ala-, Thr-, Gly-, Val- and Cys- N-termini after Met-cleavage. In humans, the homologues hNaa15p (hNat1) and hNaa10p (hArd1) were demonstrated to form a stable ribosome associated NAT complex acetylating NatA type N-termini in vitro and in vivo. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Norway | 3 | 9% |
Unknown | 30 | 91% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 7 | 21% |
Student > Master | 6 | 18% |
Student > Ph. D. Student | 4 | 12% |
Student > Bachelor | 3 | 9% |
Professor | 2 | 6% |
Other | 6 | 18% |
Unknown | 5 | 15% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 15 | 45% |
Biochemistry, Genetics and Molecular Biology | 9 | 27% |
Computer Science | 1 | 3% |
Immunology and Microbiology | 1 | 3% |
Medicine and Dentistry | 1 | 3% |
Other | 1 | 3% |
Unknown | 5 | 15% |