Modulating protein activity and cellular function by methionine residue oxidation

Cui, Zong Jie; Han, Zong Qiang; Li, Zhi Ying

doi:10.1007/s00726-011-1175-9

Cited by 47 publications

(52 citation statements)

References 102 publications

(124 reference statements)

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“…S3). However, these observed flat profiles in protein abundance do not necessarily indicate flat activity because, for example, newly synthesized proteins can be more active than old oxidized proteins (22)(23)(24). Therefore, total protein level quantified by mass spectrometry may not always reflect rhythmic activity of newly synthesized protein originating from rhythmic RFP accumulation.…”

Section: Resultsmentioning

confidence: 99%

Circadian and feeding rhythms differentially affect rhythmic mRNA transcription and translation in mouse liver

Atger

Gobet

Marquis

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

217

287

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Diurnal oscillations of gene expression are a hallmark of rhythmic physiology across most living organisms. Such oscillations are controlled by the interplay between the circadian clock and feeding rhythms. Although rhythmic mRNA accumulation has been extensively studied, comparatively less is known about their transcription and translation. Here, we quantified simultaneously temporal transcription, accumulation, and translation of mouse liver mRNAs under physiological light-dark conditions and ad libitum or night-restricted feeding in WT and brain and muscle Arnt-like 1 (Bmal1)-deficient animals. We found that rhythmic transcription predominantly drives rhythmic mRNA accumulation and translation for a majority of genes. Comparison of wild-type and Bmal1 KO mice shows that circadian clock and feeding rhythms have broad impact on rhythmic gene expression, Bmal1 deletion affecting surprisingly both transcriptional and posttranscriptional levels. Translation efficiency is differentially regulated during the diurnal cycle for genes with 5′-Terminal Oligo Pyrimidine tract (5′-TOP) sequences and for genes involved in mitochondrial activity, many harboring a Translation Initiator of Short 5′-UTR (TISU) motif. The increased translation efficiency of 5′-TOP and TISU genes is mainly driven by feeding rhythms but Bmal1 deletion also affects amplitude and phase of translation, including TISU genes. Together this study emphasizes the complex interconnections between circadian and feeding rhythms at several steps ultimately determining rhythmic gene expression and translation.circadian rhythms | ribosome profiling | mRNA translation | 5′-TOP sequences | TISU motifs L iving organisms on Earth are subjected to light-dark cycles caused by rotation of the Earth around the sun. To anticipate these changes, virtually all organisms have acquired a circadian timing system during evolution that allows a better adaptation to their environment. As a consequence, most aspects of their physiology are orchestrated in a rhythmic way by the circadian clock (from the Latin circa diem, meaning "about a day"), an endogenous and autonomous oscillator with a period of around 24 h (1, 2). Not surprisingly, perturbations of this clock in mammals lead to pathologies including psychiatric, metabolic, and vascular disorders (1,3,4). At the organismal scale, the oscillatory clockwork is organized in a hierarchal manner. Within the suprachiasmatic nuclei (SCN) of the hypothalamus, the "master clock" receives light input via the retina and communicates timing signals to "enslave" oscillators in peripheral organs (1, 2). The molecular oscillator consists of interconnected transcriptional and translational feedback loops, in which multiple layers of control, including temporal posttranscriptional and posttranslational regulation, play important roles (5). These additional layers of regulation are largely coordinated by systemic cues originating from circadian clock and/or feeding-coordinated rhythmic metabolism, allowing the adjustment of the molecular clo...

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Section: Resultsmentioning

confidence: 99%

Circadian and feeding rhythms differentially affect rhythmic mRNA transcription and translation in mouse liver

Atger

Gobet

Marquis

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

217

287

View full text Add to dashboard Cite

show abstract

“…Accordingly, it becomes intriguing how circadian function can depend on such small amplitudes. However, protein abundance does not necessarily correlate with activity, because for example, newly synthesized proteins are potentially more active than old oxidized proteins (36). Activity may, therefore, exhibit higher amplitude because of a shorter-lived newly synthesized protein pool.…”

Section: Discussionmentioning

confidence: 99%

Circadian clock-dependent and -independent rhythmic proteomes implement distinct diurnal functions in mouse liver

Mauvoisin

Wang

Jouffe

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

298

365

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Diurnal oscillations of gene expression controlled by the circadian clock underlie rhythmic physiology across most living organisms. Although such rhythms have been extensively studied at the level of transcription and mRNA accumulation, little is known about the accumulation patterns of proteins. Here, we quantified temporal profiles in the murine hepatic proteome under physiological lightdark conditions using stable isotope labeling by amino acids quantitative MS. Our analysis identified over 5,000 proteins, of which several hundred showed robust diurnal oscillations with peak phases enriched in the morning and during the night and related to core hepatic physiological functions. Combined mathematical modeling of temporal protein and mRNA profiles indicated that proteins accumulate with reduced amplitudes and significant delays, consistent with protein half-life data. Moreover, a group comprising about one-half of the rhythmic proteins showed no corresponding rhythmic mRNAs, indicating significant translational or posttranslational diurnal control. Such rhythms were highly enriched in secreted proteins accumulating tightly during the night. Also, these rhythms persisted in clock-deficient animals subjected to rhythmic feeding, suggesting that food-related entrainment signals influence rhythms in circulating plasma factors.circadian rhythm | proteomics | liver metabolism | posttranslational regulation | protein secretion L ight and heat, the principle energy sources for life, are only periodically available with a period of 1 d. Consequently, organisms acquired a timing system to adapt their physiology and anticipate these diurnal variations. In mammals, this circadian clock influences most aspects of physiology and behavior (1). In humans, perturbations of this clock lead to pathologies, including metabolic and vascular diseases. Although the oscillatory clockwork is cell-autonomous, timing on the scale of organisms uses a hierarchal organization: a master clock within the suprachiasmatic nuclei (SCN) of the hypothalamus receives light input through the retina and communicates timing signals to slave oscillators in other peripheral tissues (2).In mammals, the molecular oscillator uses interconnected transcriptional and translational feedback loops, in which multiple layers of control, including temporal posttranscriptional and posttranslational regulation, play important roles (3). An active area of chronobiology aims at understanding how the temporal signals from the core oscillator are relayed to clock output function. In this context, genome-wide rhythms in mRNA accumulation were characterized in several models. In general, around 10% of the genes, encoding many enzymes involved in different aspects of cellular metabolism, show rhythmic mRNA accumulation, establishing the role of the circadian clock in temporally gating rhythmic physiology (4).However, comparatively little is known on the temporal accumulation of proteins, despite increasing evidence suggesting that posttranscriptional mechanisms also contr...

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“…In particular, Met oxidation and subsequent reduction by Met sulfoxide reductase have far-reaching implications in metabolic, cardiovascular, neurological, and immune related dysfunction [10, 11, 12]. We have identified specific Met residues in proteins as targets of oxidation in muscle contractile and regulatory proteins [13, 14, 15].…”

Section: Introductionmentioning

confidence: 99%

Impact of methionine oxidation on calmodulin structural dynamics

McCarthy

Thompson

Nitu

et al. 2015

Biochemical and Biophysical Research Communications

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We have used electron paramagnetic resonance (EPR) to examine the structural impact of oxidizing specific methionine (M) side chains in calmodulin (CaM). It has been shown that oxidation of either M109 or M124 in CaM diminishes CaM regulation of the muscle calcium release channel, the ryanodine receptor (RyR), and that mutation of M to Q (glutamine) in either case produces functional effects identical to those of oxidation. Here we have used site-directed spin labeling and double electron-electron resonance (DEER), a pulsed EPR technique that measures distances between spin labels, to characterize the structural changes resulting from these mutations. Spin labels were attached to a pair of introduced cysteine residues, one in the C-lobe (T117C) and one in the N-lobe (T34C) of CaM, and DEER was used to determine the distribution of interspin distances. Ca binding induced a large increase in the mean distance, in concert with previous x-ray crystallography and NMR data, showing a closed structure in the absence of Ca and an open structure in the presence of Ca. DEER revealed additional information about CaM’s structural heterogeneity in solution: In both the presence and absence of Ca, CaM populates both structural states, one with probes separated by ~4 nm (closed) and another at ~6 nm (open). Ca shifts the structural equilibrium constant toward the open state by a factor of 13. DEER reveals the distribution of interprobe distances, showing that each of these states is itself partially disordered, with the width of each population ranging from 1.5 to 3 nm. Both mutations (M109Q and M124Q) decrease the effect of Ca on the structure of CaM, primarily by decreasing the closed-to-open equilibrium constant in the presence of Ca. We propose that Met oxidation alters CaM’s functional interaction with its target proteins by perturbing this Ca-dependent structural shift.

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Modulating protein activity and cellular function by methionine residue oxidation

Cited by 47 publications

References 102 publications

Circadian and feeding rhythms differentially affect rhythmic mRNA transcription and translation in mouse liver

Circadian and feeding rhythms differentially affect rhythmic mRNA transcription and translation in mouse liver

Circadian clock-dependent and -independent rhythmic proteomes implement distinct diurnal functions in mouse liver

Impact of methionine oxidation on calmodulin structural dynamics

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