First comprehensive analysis of lysine acetylation in Alvinocaris longirostris from the deep-sea hydrothermal vents.
BACKGROUND
Deep-sea hydrothermal vents are unique chemoautotrophic ecosystems with harsh conditions. Alvinocaris longirostris is one of the dominant crustacean species inhabiting in these extreme environments. It is significant to clarify mechanisms in their adaptation to the vents. Lysine acetylation has been known to play critical roles in the regulation of many cellular processes. However, its function in A. longirostris and even marine invertebrates remains elusive. Our study is the first, to our knowledge, to comprehensively investigate lysine acetylome in A. longirostris.


RESULTS
In total, 501 unique acetylation sites from 206 proteins were identified by combination of affinity enrichment and high-sensitive-massspectrometer. It was revealed that Arg, His and Lys occurred most frequently at the + 1 position downstream of the acetylation sites, which were all alkaline amino acids and positively charged. Functional analysis revealed that the protein acetylation was involved in diverse cellular processes, such as biosynthesis of amino acids, citrate cycle, fatty acid degradation and oxidative phosphorylation. Acetylated proteins were found enriched in mitochondrion and peroxisome, and many stress response related proteins were also discovered to be acetylated, like arginine kinases, heat shock protein 70, and hemocyanins. In the two hemocyanins, nine acetylation sites were identified, among which one acetylation site was unique in A. longirostris when compared with other shallow water shrimps. Further studies are warranted to verify its function.


CONCLUSION
The lysine acetylome of A. longirostris is investigated for the first time and brings new insights into the regulation function of the lysine acetylation. The results supply abundant resources for exploring the functions of acetylation in A. longirostris and other shrimps.
['Hui|Min|M|', 'Cheng|Jiao|J|', 'Sha|Zhongli|Z|http://orcid.org/0000-0002-2192-3758']
D000107:Acetylation D000222:Adaptation, Physiological D000595:Amino Acid Sequence D000818:Animals D060829:Arthropod Proteins D002851:Chromatography, High Pressure Liquid D033364:Decapoda D006433:Hemocyanins D060086:Hydrothermal Vents D008239:Lysine D008928:Mitochondria D010455:Peptides D020675:Peroxisomes D017386:Sequence Homology, Amino Acid D013312:Stress, Physiological D053719:Tandem Mass Spectrometry
Lysine acetylation Hydrothermal vent Hemocyanins Alvinocarididae Post-translational modification