BackgroundEukaryotic cells contain a huge variety of internally specialized subcellular compartments. Stoichiogenomics aims to reveal patterns of elements usage in biological macromolecules. However, the stoichiogenomic characteristics and how they adapt to various subcellular microenvironments are still unknown.ResultsHere we first updated the definition of stoichiogenomics. Then we applied it to subcellular research, and detected distinctive nitrogen content of nuclear and hydrogen, sulfur content of extracellular proteomes. Specially, we found that acidic amino acids (AAs) content of cytoskeletal proteins is the highest. The increased charged AAs are mainly caused by the eukaryotic originated cytoskeletal proteins. Functional subdivision of the cytoskeleton showed that activation, binding/association, and complexes are the three largest functional categories. Electrostatic interaction analysis showed an increased electrostatic interaction between both primary sequences and PPI interfaces of 3D structures, in the cytoskeleton.ConclusionsThis study creates a blueprint of subcellular stoichiogenomic characteristics, and explains that charged AAs of the cytoskeleton increased greatly in evolution, which offer material basis for the eukaryotic cytoskeletal proteins to act in two ways of electrostatic interactions, and further perform their activation, binding/association and complex formation.Electronic supplementary materialThe online version of this article (10.1186/s12864-018-4845-0) contains supplementary material, which is available to authorized users.
Stomach cancer involves hypoxia-specific microenvironments. Stoichiogenomics explores environmental resource limitation on biological macromolecules in terms of element usages. However, the patterns of oxygen usage by proteins and the ways that proteins adapt to a cancer hypoxia microenvironment are still unknown. Here we compared the oxygen and carbon contents ([C]) between proteomes of stomach cancer (hypoxia) and two stomach glandular cells (normal). Key proteins, genome locations, pathways, and functional dissection associated with stomach cancer were also studied. An association of oxygen content ([O]) and protein expression level was revealed in stomach cancer and stomach glandular cells. For differentially expressed proteins (DEPs), oxygen contents in the up regulated proteins were3.2%higherthan that in the down regulated proteins in stomach cancer. A total of 1,062 DEPs were identified; interestingly none of these proteins were coded on Y chromosome. The up regulated proteins were significantly enriched in pathways including regulation of actin cytoskeleton, cardiac muscle contraction, pathway of progesterone-mediated oocyte maturation, etc. Functional dissection of the up regulated proteins with high oxygen contents showed that most of them were cytoskeleton, cytoskeleton associated proteins, cyclins and signaling proteins in cell cycle progression. Element signature of resource limitation could not be detected in stomach cancer for oxygen, just as what happened in plants and microbes. Unsaved use of oxygen by the highly expressed proteins was adapted to the rapid growth and fast division of the stomach cancer cells. In addition, oxygen usage bias, key proteins and pathways identified in this paper laid a foundation for application of stoichiogenomics in precision medicine.
Hypoxia plays a critical role in melanoma development, but the characteristics of elemental oxygen in proteins and adaptation to hypoxia microenvironments are still unidentified. This study aims to explore oxygen contents (OCs) and differentially expressed proteins (DEP). Protein expression data were retrieved from Human Protein Atlas. The DEP in melanoma samples were compared with normal skin cells. We identified 1,969 DEP, and none of the genes coding these proteins were present on chromosome Y. The average oxygen content (AOC) was 7.24% higher in highly expressed proteins than lowly expressed proteins in melanoma and normal skin cells. The AOC is 2.36% higher in the up regulated proteins (URPs) in melanoma. The essential amino acids in the proteins in melanoma cells contributed to increased OC. Functional dissections of the high OCs in URP displayed that some of these proteins are associated with cytoskeleton, cyclins and cell cycle proteins. The URP interactions were generated using a STRING database. Majority of these URPs are associated in expression, exhibiting sufficient interactions with each other. This study provides useful information regarding protein expression in melanoma cells and the molecular mechanism of melanoma using stoichiogenomics.
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