scholarly journals The SUMO ligase MMS21 profoundly influences maize development through its impact on genome activity and stability

PLoS Genetics ◽  
2021 ◽  
Vol 17 (10) ◽  
pp. e1009830
Author(s):  
Junya Zhang ◽  
Robert C. Augustine ◽  
Masaharu Suzuki ◽  
Juanjuan Feng ◽  
Si Nian Char ◽  
...  
Keyword(s):  
Dna Repair ◽  
Seed Storage Protein ◽  
Ectopic Expression ◽  
Seed Storage ◽  
Vegetative Development ◽  
Chromatin Dynamics ◽  
Sumo Ligase ◽  
High Ploidy ◽  
Genome Activity

The post-translational addition of SUMO plays essential roles in numerous eukaryotic processes including cell division, transcription, chromatin organization, DNA repair, and stress defense through its selective conjugation to numerous targets. One prominent plant SUMO ligase is METHYL METHANESULFONATE-SENSITIVE (MMS)-21/HIGH-PLOIDY (HPY)-2/NON-SMC-ELEMENT (NSE)-2, which has been connected genetically to development and endoreduplication. Here, we describe the potential functions of MMS21 through a collection of UniformMu and CRISPR/Cas9 mutants in maize (Zea mays) that display either seed lethality or substantially compromised pollen germination and seed/vegetative development. RNA-seq analyses of leaves, embryos, and endosperm from mms21 plants revealed a substantial dysregulation of the maize transcriptome, including the ectopic expression of seed storage protein mRNAs in leaves and altered accumulation of mRNAs associated with DNA repair and chromatin dynamics. Interaction studies demonstrated that MMS21 associates in the nucleus with the NSE4 and STRUCTURAL MAINTENANCE OF CHROMOSOMES (SMC)-5 components of the chromatin organizer SMC5/6 complex, with in vitro assays confirming that MMS21 will SUMOylate SMC5. Comet assays measuring genome integrity, sensitivity to DNA-damaging agents, and protein versus mRNA abundance comparisons implicated MMS21 in chromatin stability and transcriptional controls on proteome balance. Taken together, we propose that MMS21-directed SUMOylation of the SMC5/6 complex and other targets enables proper gene expression by influencing chromatin structure.

scholarly journals Processing Pisum sativum seed storage protein precursors in vitro

Cell Research ◽  
1990 ◽  
Vol 1 (2) ◽  
pp. 153-162 ◽  
Author(s):  
Lijun Yang ◽  
C Domoney ◽  
R Casey ◽  
TC Hall
Keyword(s):  
Pisum Sativum ◽  
Storage Protein ◽  
Seed Storage Protein ◽  
Seed Storage

scholarly journals Human MMS21/NSE2 Is a SUMO Ligase Required for DNA Repair

2005 ◽  
Vol 25 (16) ◽  
pp. 7021-7032 ◽  
Author(s):  
Patrick Ryan Potts ◽  
Hongtao Yu
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Ectopic Expression ◽  
Well Being ◽  
Dna Lesions ◽  
Wild Type ◽  
Sumo Ligase ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Induced Apoptosis

ABSTRACT DNA repair is required for the genomic stability and well-being of an organism. In yeasts, a multisubunit complex consisting of SMC5, SMC6, MMS21/NSE2, and other non-SMC proteins is required for DNA repair through homologous recombination. The yeast MMS21 protein is a SUMO ligase. Here we show that the human homolog of MMS21 is also a SUMO ligase. hMMS21 stimulates sumoylation of hSMC6 and the DNA repair protein TRAX. Depletion of hMMS21 by RNA interference (RNAi) sensitizes HeLa cells toward DNA damage-induced apoptosis. Ectopic expression of wild-type hMMS21, but not its ligase-inactive mutant, rescues this hypersensitivity of hMMS21-RNAi cells. ATM/ATR are hyperactivated in hMMS21-RNAi cells upon DNA damage. Consistently, hMMS21-RNAi cells show an increased number of phospho-CHK2 foci. Finally, we show that hMMS21-RNAi cells show a decreased capacity to repair DNA lesions as measured by the comet assay. Our findings suggest that the human SMC5/6 complex and the SUMO ligase activity of hMMS21 are required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair in human cells.

scholarly journals The macrocyclizing protease butelase 1 remains auto-catalytic and reveals the structural basis for ligase activity

2018 ◽  
Author(s):  
Amy M. James ◽  
Joel Haywood ◽  
Julie Leroux ◽  
Katarzyna Ignasiak ◽  
Alysha G. Elliott ◽  
...  
Keyword(s):  
Active Site ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Structural Basis ◽  
Evolutionary Constraint ◽  
Catalytic Cleavage ◽  
Ph Conditions ◽  
The Many

AbstractPlant asparaginyl endopeptidases (AEPs) are expressed as inactive zymogens that perform seed storage protein maturation upon cleavage dependent auto-activation in the low pH environment of storage vacuoles. AEPs have attracted attention for their macrocyclization reactions and have been classified as cleavage or ligation specialists. However, we have recently shown that the ability of AEPs to produce either cyclic or acyclic products can be altered by mutations to the active site region, and that several AEPs are capable of macrocyclization given favorable pH conditions. One AEP extracted from Clitoria ternatea seeds (butelase 1) is classified as a ligase rather than a protease, presenting an opportunity to test for loss of cleavage activity. Here, making recombinant butelase 1 and rescuing an Arabidopsis thaliana mutant lacking AEP, we show butelase 1 retains cleavage functions in vitro and in vivo. The in vivo rescue was incomplete, consistent with some trade-off for butelase 1 specialization toward macrocyclization. Its crystal structure showed an active site with only subtle differences from cleaving AEPs, suggesting the many differences in its peptide binding region are the source of its efficient macrocyclization. All considered, it seems either butelase 1 has not fully specialized or a requirement for auto-catalytic cleavage is an evolutionary constraint upon macrocyclizing AEPs.

RECONSTRUCTION OF DNA-REPAIR DEFICIENT XERODERMA PIGMENTOSUM SKIN IN VITRO: A MODEL TO STUDY HYPERSENSITIVITY TO UV LIGHT

2004 ◽  
Author(s):  
Françoise Bernerd ◽  
Daniel Asselineau ◽  
Mathilde Frechet ◽  
Alain Sarasin ◽  
Thierry Magnaldo
Keyword(s):  
Dna Repair ◽  
Xeroderma Pigmentosum ◽  
Uv Light

Chromatin dynamics and DNA repair

10.2741/1013 ◽  
2003 ◽  
Vol 8 (6) ◽  
pp. s149-155 ◽  
Author(s):  
Vasily V Ogryzko
Keyword(s):  
Dna Repair ◽  
Chromatin Dynamics

Pharmacological targeting of differential DNA repair, radio-sensitizes WRN-deficient cancer cells in vitro and in vivo

2021 ◽  
Vol 186 ◽  
pp. 114450
Author(s):  
Pooja Gupta ◽  
Bhaskar Saha ◽  
Subrata Chattopadhyay ◽  
Birija Sankar Patro
Keyword(s):  
Dna Repair ◽  
Cancer Cells

scholarly journals Molecular cytogenetical and biochemical studies on some Lupinus species

2021 ◽  
Vol 45 (1) ◽  
Author(s):  
Hoda B. M. Ali ◽  
Samy A. A. Heiba
Keyword(s):  
Related Species ◽  
Storage Protein ◽  
Seed Storage Protein ◽  
Lupinus Albus ◽  
Seed Storage ◽  
Rrna Genes ◽  
Large Chromosome ◽  
45S Rdna ◽  
Lupinus Polyphyllus ◽  
Electrophoretic Patterns

Abstract Background Lupins are cultivated as human consumption grains and forage legumes. The chromosomes of lupins are too small to be karyotyped by conventional techniques, because they reveal a general lack of distinctive cytological features. In the current study, Fluorescence in situ Hybridization (FISH) was used to locate 5S and 45S ribosomal gene sites on the chromosomes of Lupinus albus ssp albus, Lupinus albus ssp graecus, Lupnus termis (all with 2n = 50), and Lupinus polyphyllus lindl var. polyphyllus (2n = 48), FISH together with seed storage protein electrophoretic patterns were used to find out the relationship among these species. Results The double-target FISH on the chromosomes of the studied species with rDNA probes revealed that the two types of rRNA genes are located on different chromosomes. The detected loci of rRNA genes partially reflected the taxonomical similarity among the two Lupinus albus subspecies and L. termis. Lupinus polyphyllus lindl var. polyphyllus was exception by having unique large chromosome mostly is covered by one signal of 45S rDNA, whereas its homologous chromosome seems to be normal-sized and have the other 45S rDNA locus. The similarity matrix among the Lupinus species as computed according to Jaccardʼs Coefficient from the SDS-PAGE, showed that L. albus ssp. Albus and L. albus ssp. Graecus are the most similar species (~ 97%), and then comes L. termis, and L. polyphyllus lindl var. polyphylus has been placed in separate clade and still the most related species to it among the studied species is L. termis (~ 70%). Conclusion It could be postulated from FISH and seed storage protein electrophoretic patterns that the relationships among the studied species is as follows, Lupinus albus ssp albus, is the most related species to Lupinus albus ssp graecus then comes Lupnus termis and Lupinus polyphyllus lindl var. polyphyllus at a distal position.

Sign in / Sign up

Export Citation Format

Share Document