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Invadolysin acts genetically via the SAGA complex to modulate chromosome structure.

Rao SG, Janiszewski MM, Duca E, Nelson B, Abhinav K, Panagakou I, Vass S, Heck MM - Nucleic Acids Res. (2015)

Bottom Line: Over-expression of the Bre1 ubiquitin ligase phenocopies the effects of mutating either the invadolysin or nonstop genes.We further suggest that the mislocalization of ubH2B to the cytoplasm has additional consequences on downstream components essential for chromosome behaviour.We therefore propose that invadolysin plays a crucial role in chromosome organization via its interaction with the SAGA complex.

View Article: PubMed Central - PubMed

Affiliation: University of Edinburgh, Queen's Medical Research Institute, University/BHF Centre for Cardiovascular Science, 47 Little France Crescent, Edinburgh EH16 4TJ, UK.

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Model for the interaction between invadolysin, nonstop and bre1. We hypothesize that invadolysin affects higher order chromosome architecture through an effect on the balance of histone modification. Ubiquitination of histone H2B is accomplished through the concerted action of the bre1 ubiquitin ligase and the nonstop ubiquitinating protease. In the absence of invadolysin, we speculate there is decreased activity of nonstop, which would result in the accumulation of ubiquitinated H2B. In nonstop and invadolysin mutants, and in animals where Bre1 is overexpressed, ubH2B, H3K4me3, H3K4me2 and H3K9/14ac accumulate and abnormally-structured chromosomes are observed.
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Figure 8: Model for the interaction between invadolysin, nonstop and bre1. We hypothesize that invadolysin affects higher order chromosome architecture through an effect on the balance of histone modification. Ubiquitination of histone H2B is accomplished through the concerted action of the bre1 ubiquitin ligase and the nonstop ubiquitinating protease. In the absence of invadolysin, we speculate there is decreased activity of nonstop, which would result in the accumulation of ubiquitinated H2B. In nonstop and invadolysin mutants, and in animals where Bre1 is overexpressed, ubH2B, H3K4me3, H3K4me2 and H3K9/14ac accumulate and abnormally-structured chromosomes are observed.

Mentions: Based on our results, we propose the model in Figure 8 for the role of invadolysin in higher-order chromosome structure. Invadolysin may work to balance the dBre1 [ubiquitinating] and nonstop [deubiquitinating] activities to regulate histone ubiquitination and ensuing chromosomal architecture. When ubH2B accumulates in the cytoplasm or on mitotic chromosomes, chromosome structure is affected, such that chromosomes appear hypercondensed in length, yet fuzzy in periphery. Cytoplasmic ubH2B accumulation may also result in changes in transcription via the accumulation of H3K4me3. We have not yet determined whether the genetic interaction described herein is also mirrored by direct physical interaction between invadolysin and SAGA complex subunits.


Invadolysin acts genetically via the SAGA complex to modulate chromosome structure.

Rao SG, Janiszewski MM, Duca E, Nelson B, Abhinav K, Panagakou I, Vass S, Heck MM - Nucleic Acids Res. (2015)

Model for the interaction between invadolysin, nonstop and bre1. We hypothesize that invadolysin affects higher order chromosome architecture through an effect on the balance of histone modification. Ubiquitination of histone H2B is accomplished through the concerted action of the bre1 ubiquitin ligase and the nonstop ubiquitinating protease. In the absence of invadolysin, we speculate there is decreased activity of nonstop, which would result in the accumulation of ubiquitinated H2B. In nonstop and invadolysin mutants, and in animals where Bre1 is overexpressed, ubH2B, H3K4me3, H3K4me2 and H3K9/14ac accumulate and abnormally-structured chromosomes are observed.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4402531&req=5

Figure 8: Model for the interaction between invadolysin, nonstop and bre1. We hypothesize that invadolysin affects higher order chromosome architecture through an effect on the balance of histone modification. Ubiquitination of histone H2B is accomplished through the concerted action of the bre1 ubiquitin ligase and the nonstop ubiquitinating protease. In the absence of invadolysin, we speculate there is decreased activity of nonstop, which would result in the accumulation of ubiquitinated H2B. In nonstop and invadolysin mutants, and in animals where Bre1 is overexpressed, ubH2B, H3K4me3, H3K4me2 and H3K9/14ac accumulate and abnormally-structured chromosomes are observed.
Mentions: Based on our results, we propose the model in Figure 8 for the role of invadolysin in higher-order chromosome structure. Invadolysin may work to balance the dBre1 [ubiquitinating] and nonstop [deubiquitinating] activities to regulate histone ubiquitination and ensuing chromosomal architecture. When ubH2B accumulates in the cytoplasm or on mitotic chromosomes, chromosome structure is affected, such that chromosomes appear hypercondensed in length, yet fuzzy in periphery. Cytoplasmic ubH2B accumulation may also result in changes in transcription via the accumulation of H3K4me3. We have not yet determined whether the genetic interaction described herein is also mirrored by direct physical interaction between invadolysin and SAGA complex subunits.

Bottom Line: Over-expression of the Bre1 ubiquitin ligase phenocopies the effects of mutating either the invadolysin or nonstop genes.We further suggest that the mislocalization of ubH2B to the cytoplasm has additional consequences on downstream components essential for chromosome behaviour.We therefore propose that invadolysin plays a crucial role in chromosome organization via its interaction with the SAGA complex.

View Article: PubMed Central - PubMed

Affiliation: University of Edinburgh, Queen's Medical Research Institute, University/BHF Centre for Cardiovascular Science, 47 Little France Crescent, Edinburgh EH16 4TJ, UK.

Show MeSH
Related in: MedlinePlus