Characterization of mouse ubiquitin‐like SMT3A and SMT3B cNDAS and gene/pseudogenes

  title={Characterization of mouse ubiquitin‐like SMT3A and SMT3B cNDAS and gene/pseudogenes},
  author={A. Y. Chen and Hideyuki Mannen and S. S. Li},
  journal={IUBMB Life},
Mouse SMT3A and SMT3B cDNAs encoding ubiquitin‐like proteins of 110 and 95 amino acids, respectively, were isolated and sequenced. The sequence of the first 92 amino acids (ending with the conserved Gly‐Gly) of mouse SMT3A exhibited two differences at amino acid no. 38 and 76 in comparison with that of human SMT3A. The C‐terminal 18 amino acid sequence of mouse SMT3A was completely different The nucleotide sequences have been deposited in the GenBank database (SMT3A cDNA, AF063847; SMT3A‐pg1… Expand
Functional Heterogeneity of Small Ubiquitin-related Protein Modifiers SUMO-1 versus SUMO-2/3*
Qualitative and qualitative results support the concept of important distinctions between thesumO-2/3 and SUMO-1 conjugation pathways and suggest a role for SUMO/3 in the cellular responses to environmental stress. Expand
Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.
Most SUMO-1/2/3 proteins were shown to be localized on nuclear membrane, nuclear bodies and cytoplasm, respectively, while many cellular proteins of high molecular weights were covalently modified bysumolyzation. Expand
Small ubiquitin-related modifier-1: Wrestling with protein regulation.
  • J. Barry, R. Lock
  • Biology, Medicine
  • The international journal of biochemistry & cell biology
  • 2011
This work has shown that dysregulated SUMOylation has been implicated in several neurodegenerative disorders, heart disease and cancer, and highlights the need for further research but also the potential of SUMO-1 as a therapeutic target. Expand
Evaluation of the activity and substrate specificity of the human SENP family of SUMO proteases.
It is found that SENP1 is by far the most versatile and active SENP whereas SENP3 stands out as the least active of these enzymes. Expand
A genetic screen to discover SUMOylated proteins in living mammalian cells
A method to screen for mammalian SUMOylated proteins using the reconstitution of split fluorescent protein fragments in living mammalian cells and successfully identified 36 unreported SUMO2-substrate candidates with distinct intracellular localizations and functions is developed. Expand
SUMO and SUMOylation in plants
Results of recent insights into the role of sumoylation in plants are discussed and further SUMO noncovalent binding appears to have function in other model organisms and SUMO interacting proteins in plants will be of interest to plant biologists who dissect the dynamic function of SUMO. Expand
Characterization of a Fission Yeast SUMO-1 Homologue, Pmt3p, Required for Multiple Nuclear Events, Including the Control of Telomere Length and Chromosome Segregation
The identification of the SUMO-1 homologue of fission yeast, which is shown to be required for a number of nuclear events including the control of telomere length and chromosome segregation, suggests that several nuclear proteins are regulated by Pmt3p conjugation. Expand
Sumoylation regulates diverse biological processes
  • J. Zhao
  • Biology, Medicine
  • Cellular and Molecular Life Sciences
  • 2007
This paper reviews recent progress in the study of SUMO pathways, substrates, and cellular functions and highlights important findings that have accelerated advances in this study field and link sumoylation to human diseases. Expand
SUMOylation of Myc-Family Proteins
It is shown that c- and N-Myc are conjugated to SUMO proteins at conserved lysines in their C-terminal domain, and it is surmise that, as shown for other substrates, SUMOylation may be part of a quality-control mechanism acting on misfolded Myc proteins. Expand
Comparative proteomic analysis identifies protein disulfide isomerase and peroxiredoxin 1 as new players involved in embryonic interdigital cell death
  • S. Shan, M. Tang, +4 authors K. H. Lee
  • Biology, Medicine
  • Developmental dynamics : an official publication of the American Association of Anatomists
  • 2005
This study identifies two new players in interdigital cell death and highlights that PCD is regulated by a delicate balance of proapoptotic and survival‐promoting activities. Expand