Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro

Purohit, Jogeswar S.; Tomar, Raghuvir Singh; Panigrahi, Anil K.; Pandey, Shashibhal M.; Singh, Divya; Chaturvedi, Madan M.

doi:10.1016/j.biochi.2013.07.005

Cited by 19 publications

(13 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…An additional but less abundant Prb1 cleavage site in H3 is located between Lys27 and Ser28. Interestingly, GDH and Cathepsin L also cleavage histone H3 at the same sites (Lys23/Ala24 and Lys27/Ser28) [18], [19], [20] which is consistent with our result. We also detected some intact H3 N-terminal sequence (ARTKQT) in truncated H3, which indicates that a fraction of truncated H3 resulted from cleavage at the C terminus but we did not see cleavage in vitro of recombinant yeast H3 between Ala21 and Ser22.…”

Section: Resultssupporting

confidence: 92%

“…For example, in Saccharomyces cerevisiae , a serine protease activity is present that cleaves the histone H3 tail after Ala21 in sporulation and stationary phase, and preventing truncation using a mutation H3 Q19A, L20A results in decreased transcription of selected yeast genes in stationary phase [16]. In chicken, a tissue-specific histone H3 N-terminal cleavage activity was found in adult chicken liver that has been connected to gene expression during aging [17] and later it was identified as GDH (Glutamate dehydrogenase) which cleaves H3 between Lys23 and Ala24 [18], [19]. Finally, mouse cathepsin L, a lysosomal cysteine protease, is required for the cleavage of H3 tails between residues 21–27 during embryonic stem cell differentiation [20].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

PRB1 Is Required for Clipping of the Histone H3 N Terminal Tail in Saccharomyces cerevisiae

et al. 2014

View full text Add to dashboard Cite

Cathepsin L, a lysosomal protein in mouse embryonic stem cells has been shown to clip the histone H3 N- terminus, an activity associated with gene activity during mouse cell development. Glutamate dehydrogenase (GDH) was also identified as histone H3 specific protease in chicken liver, which has been connected to gene expression during aging. In baker’s yeast, Saccharomyces cerevisiae, clipping the histone H3 N-terminus has been associated with gene activation in stationary phase but the protease responsible for the yeast histone H3 endopeptidase activity had not been identified. In searching for a yeast histone H3 endopeptidase, we found that yeast vacuolar protein Prb1 is present in the cellular fraction enriched for the H3 N-terminus endopeptidase activity and this endopeptidase activity is lost in the PRB1 deletion mutant (prb1Δ). In addition, like Cathepsin L and GDH, purified Prb1 from yeast cleaves H3 between Lys23 and Ala24 in the N-terminus in vitro as shown by Edman degradation. In conclusion, our data argue that PRB1 is required for clipping of the histone H3 N-terminal tail in Saccharomyces cerevisiae.

show abstract

Section: Resultssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

PRB1 Is Required for Clipping of the Histone H3 N Terminal Tail in Saccharomyces cerevisiae

et al. 2014

View full text Add to dashboard Cite

show abstract

“…In particular, the mitochondrial enzyme is solubilized in 0.25 M sucrose while the solubilization of the nuclear isoform requires the addition of 0.1 M potassium phosphate [26]. A recent study of chicken liver GDH [31] confirmed the nuclear localization of this enzyme [26,27,28,29] by uncovering the ability of GDH to act as a serine protease of histone H3 [31]. GDH was also found in the granular endoplasmic reticulum of rat liver [32].…”

Section: Intracellular Localization Of Gdh In Animalsmentioning

confidence: 99%

“…Recent data on both the nuclear and mitochondrial localization of the single human isoenzyme hGDH1 [31,96] suggest that the observed functional differences between the mitochondrial and nuclear GDHs may be due to post-transcriptional and/or post-translational modifications (see Section 3.2 and Section 7). …”

Section: Kinetic Investigation Of Gdh and Its Isoformsmentioning

confidence: 99%

Multiple Forms of Glutamate Dehydrogenase in Animals: Structural Determinants and Physiological Implications

Bunik

Artiukhov

Aleshin

et al. 2016

Biology

View full text Add to dashboard Cite

Glutamate dehydrogenase (GDH) of animal cells is usually considered to be a mitochondrial enzyme. However, this enzyme has recently been reported to be also present in nucleus, endoplasmic reticulum and lysosomes. These extramitochondrial localizations are associated with moonlighting functions of GDH, which include acting as a serine protease or an ATP-dependent tubulin-binding protein. Here, we review the published data on kinetics and localization of multiple forms of animal GDH taking into account the splice variants, post-translational modifications and GDH isoenzymes, found in humans and apes. The kinetic properties of human GLUD1 and GLUD2 isoenzymes are shown to be similar to those published for GDH1 and GDH2 from bovine brain. Increased functional diversity and specific regulation of GDH isoforms due to alternative splicing and post-translational modifications are also considered. In particular, these structural differences may affect the well-known regulation of GDH by nucleotides which is related to recent identification of thiamine derivatives as novel GDH modulators. The thiamine-dependent regulation of GDH is in good agreement with the fact that the non-coenzyme forms of thiamine, i.e., thiamine triphosphate and its adenylated form are generated in response to amino acid and carbon starvation.

show abstract

“…Recent evidence suggests that histone H3 clipping may play an important role in senescence (Duarte et al ., ). Moreover, we have also identified glutamate dehydrogenase (GDH) as a H3‐specific protease from chicken liver (Mandal et al ., , ; Purohit et al ., ). Cathepsin L has been identified as a histone H3‐specific protease that is required for the clipping of H3 tails between residues 21–27 during the process of embryonic stem cell differentiation (Duncan et al ., ).…”

Section: Introductionmentioning

confidence: 97%

Partial purification of histone H3 proteolytic activity from the budding yeast Saccharomyces cerevisiae

Azad

Tomar

2016

Yeast

View full text Add to dashboard Cite

The proteolytic clipping of histone tails has recently emerged as a novel form of irreversible post-translational modification (PTM) of histones. Histone clipping has been implicated as a regulatory process leading to the permanent removal of PTMs from histone proteins. However, there is scarcity of literature that describes the identification and characterization of histone-specific proteases. Here, we employed various biochemical methods to report histone H3-specific proteolytic activity from budding yeast. Our results demonstrate that H3 proteolytic activity was associated with sepharose bead matrices and activity was not affected by a variety of stress conditions. We have also identified the existence of an unknown protein that acts as a physiological inhibitor of the H3-clipping activity of yeast H3 protease. Moreover, through protease inhibition assays, we have also characterized yeast H3 protease as a serine protease. Interestingly, unlike glutamate dehydrogenase (GDH), yeast H3 proteolytic activity was not inhibited by Stefin B. Together, our findings suggest the existence of a novel H3 protease in yeast that is different from other reported histone H3 proteases. The presence of histone H3 proteolytic activity, along with the physiological inhibitor in yeast, suggests an interesting molecular mechanism that regulates the activity of histone proteases.

show abstract

Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro

Cited by 19 publications

References 56 publications

PRB1 Is Required for Clipping of the Histone H3 N Terminal Tail in Saccharomyces cerevisiae

PRB1 Is Required for Clipping of the Histone H3 N Terminal Tail in Saccharomyces cerevisiae

Multiple Forms of Glutamate Dehydrogenase in Animals: Structural Determinants and Physiological Implications

Partial purification of histone H3 proteolytic activity from the budding yeast Saccharomyces cerevisiae

Contact Info

Product

Resources

About