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Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1

XU, Zheng, AU, Shannon W. N.·2005·Biochemical Journal
DOI 10.1042/bj20041210
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Abstract

SUMO (small ubiquitin-related modifier) is a member of the ubiquitin-like protein family that regulates cellular function of a variety of target proteins. SUMO proteins are expressed as their precursor forms. Cleavage of the residues after the ‘GG’ region of these precursors by SUMO-specific proteases in maturation is a prerequisite for subsequent sumoylation. To understand further this proteolytic processing, we expressed and purified SENP1 (sentrin-specific protease 1), one of the SUMO-specific proteases, using an Escherichia coli expression system. We show that SENP1 is capable of processing all SUMO-1, -2 and -3 in vitro; however, the proteolytic efficiency of SUMO-1 is the highest followed by SUMO-2 and -3. We demonstrate further that the catalytic domain of SENP1 (SENP1C) alone can determine the substrate specificity towards SUMO-1, -2 and -3. Replacement of the C-terminal fragments after the ‘GG’ region of SUMO-1 and -2 precursors with that of the SUMO-3, indicates that the C-terminal fragment is essential for efficient maturation. In mutagenesis analysis, we further map two residues immediately after the ‘GG’ region, which determine the differential maturation. Distinct patterns of tissue distribution of SENP1, SUMO-1, -2 and -3 are characterized. Taken together, we suggest that the observed differential maturation process has its physiological significance in the regulation of the sumoylation pathway.

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  • SENP1 mRNA and protein are present in many human tissues including the liver, and are highly enriched in the testis.

    “Further, SENP1 mRNA and protein, despite present in many human tissues including the liver, are highly enriched in the testis (43) (www.proteinatlas.org).”

    From SUMOylation of the ubiquitin ligase IDOL decreases LDL receptor levels and is reversed by SENP1 (2021) · cites this paper as [43]

    The ‘Distinct expression patterns’ section reports that SENP1 is highly expressed in testis and detectable in several other human tissues, including liver. However, the tissue-distribution experiment measured transcription by PCR, not SENP1 protein levels, so this source does not establish the claim about protein distribution. (LLM, conf=0.88)

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Research works printed but not linked: 37

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Metadata

Authors
XU, Z., & AU, S. W. N.
Affiliations
Department of Biochemistry, Faculty of Science, The Chinese University of Hong Kong, Shatin, Hong Kong
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2005-02-22
Volume
386
Issue
2
Pages
325-330
ISSN
  • 0264-6021
  • 1470-8728
DOI
10.1042/bj20041210
Cited by
79
References
0
Language
en

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