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    Biochem Biophys Res Commun. 1999 Apr 2;257(1):100-5.

    Identification of NEDD8-conjugation site in human cullin-2.

    Wada H, Yeh ET, Kamitani T.

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    Department of Internal Medicine, Institute of Molecular Medicine for the Prevention of Human Diseases, Houston, Texas 77030, USA.

    Abstract

    NEDD8 is a novel ubiquitin-like protein that has been shown to conjugate to nuclear proteins in a manner analogous to ubiquitination and sentrinization. Recently, human cullin-4A was reported to be conjugated by a single molecule of NEDD8. Here, we show that human cullin-2 is also conjugated by a single molecule of the NEDD8. The C-terminal 171-amino-acid residues in human cullin-2 are sufficient for NEDD8-conjugation. In addition, the equivalent C-terminal fragments of other cullins have been shown to be conjugated by NEDD8. Mapping of the NEDD8-conjugation site revealed that Lys-689 in human cullin-2 is conjugated by NEDD8. Interestingly, the Lys residue at position 689 in cullin-2 is conserved in all cullin family members, including human cullin-1, -2, -3, -4A, -4B, and -5 and yeast cullin (Cdc53), suggesting the possibility that other cullin family members are conjugated by NEDD8/Rub1 at a Lys residue of equivalent position.

    Copyright 1999 Academic Press.

    PMID:
    10092517
    [PubMed - indexed for MEDLINE]

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