Invariable stoichiometry of ribosomal proteins in mouse brain tissues with aging
Standard
Invariable stoichiometry of ribosomal proteins in mouse brain tissues with aging. / Amirbeigiarab, Susan; Kiani, Parnian; Velazquez Sanchez, Ana; Krisp, Christoph; Kazantsev, Andriy; Fester, Lars; Schlüter, Hartmut; Ignatova, Zoya.
In: P NATL ACAD SCI USA, Vol. 116, No. 45, 05.11.2019, p. 22567-22572.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
Harvard
APA
Vancouver
Bibtex
}
RIS
TY - JOUR
T1 - Invariable stoichiometry of ribosomal proteins in mouse brain tissues with aging
AU - Amirbeigiarab, Susan
AU - Kiani, Parnian
AU - Velazquez Sanchez, Ana
AU - Krisp, Christoph
AU - Kazantsev, Andriy
AU - Fester, Lars
AU - Schlüter, Hartmut
AU - Ignatova, Zoya
PY - 2019/11/5
Y1 - 2019/11/5
N2 - Across phyla, the ribosomes-the central molecular machines for translation of genetic information-exhibit an overall preserved architecture and a conserved functional core. The natural heterogeneity of the ribosome periodically phases a debate on their functional specialization and the tissue-specific variations of the ribosomal protein (RP) pool. Using sensitive differential proteomics, we performed a thorough quantitative inventory of the protein composition of ribosomes from 3 different mouse brain tissues, i.e., hippocampus, cortex, and cerebellum, across various ages, i.e., juvenile, adult, and middle-aged mouse groups. In all 3 brain tissues, in both monosomal and polysomal ribosome fractions, we detected an invariant set of 72 of 79 core RPs, RACK1 and 2 of the 8 RP paralogs, the stoichiometry of which remained constant across different ages. The amount of a few RPs punctually varied in either one tissue or one age group, but these fluctuations were within the tight bounds of the measurement noise. Further comparison with the ribosomes from a high-metabolic-rate organ, e.g., the liver, revealed protein composition identical to that of the ribosomes from the 3 brain tissues. Together, our data show an invariant protein composition of ribosomes from 4 tissues across different ages of mice and support the idea that functional heterogeneity may arise from factors other than simply ribosomal protein stoichiometry.
AB - Across phyla, the ribosomes-the central molecular machines for translation of genetic information-exhibit an overall preserved architecture and a conserved functional core. The natural heterogeneity of the ribosome periodically phases a debate on their functional specialization and the tissue-specific variations of the ribosomal protein (RP) pool. Using sensitive differential proteomics, we performed a thorough quantitative inventory of the protein composition of ribosomes from 3 different mouse brain tissues, i.e., hippocampus, cortex, and cerebellum, across various ages, i.e., juvenile, adult, and middle-aged mouse groups. In all 3 brain tissues, in both monosomal and polysomal ribosome fractions, we detected an invariant set of 72 of 79 core RPs, RACK1 and 2 of the 8 RP paralogs, the stoichiometry of which remained constant across different ages. The amount of a few RPs punctually varied in either one tissue or one age group, but these fluctuations were within the tight bounds of the measurement noise. Further comparison with the ribosomes from a high-metabolic-rate organ, e.g., the liver, revealed protein composition identical to that of the ribosomes from the 3 brain tissues. Together, our data show an invariant protein composition of ribosomes from 4 tissues across different ages of mice and support the idea that functional heterogeneity may arise from factors other than simply ribosomal protein stoichiometry.
U2 - 10.1073/pnas.1912060116
DO - 10.1073/pnas.1912060116
M3 - SCORING: Journal article
C2 - 31636180
VL - 116
SP - 22567
EP - 22572
JO - P NATL ACAD SCI USA
JF - P NATL ACAD SCI USA
SN - 0027-8424
IS - 45
ER -
