2013 journal article
Dynamics of the Striped Bass (Morone saxatilis) Ovary Proteome Reveal a Complex Network of the Translasome
JOURNAL OF PROTEOME RESEARCH, 12(4), 1691–1699.
author keywords: ribosome; proteasome; translasome; ovary; reproduction; mass-spectrometry; support vector machines; teleost; fish
MeSH headings : Animals; Artificial Intelligence; Bass; Cluster Analysis; Female; Fish Proteins / genetics; Fish Proteins / metabolism; Gene Ontology; Mass Spectrometry / methods; Menstrual Cycle / physiology; Ovary / metabolism; Proteasome Endopeptidase Complex / metabolism; Proteome / metabolism; Ribosomes / genetics; Ribosomes / metabolism
TL;DR:
The striped bass ovary proteome is evaluated using label-free quantitative mass spectrometry and a novel machine learning analysis based on K-means clustering and support vector machines to suggest that protein synthesis and degradation are intimately linked.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
14. Life Below Water
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
We evaluated changes in the striped bass (Morone saxatilis) ovary proteome during the annual reproductive cycle using label-free quantitative mass spectrometry and a novel machine learning analysis based on K-means clustering and support vector machines. Modulated modularity clustering was used to group co-variable proteins into expression modules and Gene Ontology (GO) biological process and KEGG pathway enrichment analyses were conducted for proteins within those modules. We discovered that components of the ribosome along with translation initiation and elongation factors generally decrease as the annual ovarian cycle progresses toward ovulation, concomitant with a slight increase in components of the 26S-proteasome. Co-variation within more than one expression module of components from these two multi-protein complexes suggests that they are not only co-regulated, but that co-regulation occurs through more than one sub-network. These components also co-vary with subunits of the TCP-1 chaperonin system and enzymes of intermediary metabolic pathways, suggesting that protein folding and cellular bioenergetic state play important roles in protein synthesis and degradation. We provide further evidence to suggest that protein synthesis and degradation are intimately linked, and our results support function of a proteasome-ribosome supercomplex known as the translasome.