The Arabidopsis PHD-finger protein SHL is required for proper development and fertility
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O R I GI N A L P A P E R
C. MuÈssig á A. Kauschmann á S. D. Clouse á T. Altmann
The Arabidopsis PHD-®nger protein SHL is required for proper development and fertility
Received: 17 March 2000 / Accepted: 15 June 2000 / Published online: 29 July 2000 Ó Springer-Verlag 2000
Abstract The SHL gene from Arabidopsis thaliana encodes a small nuclear protein that contains a BAH domain and a PHD ®nger. Both domains are found in numerous (putative) transcriptional regulators and chromatin-remodeling factors. Dierent sets of transgenic lines were established to analyze the physiological relevance of SHL. SHL expression driven by the CaMV 35S promoter results in reduced growth, early ¯owering, early senescence, and impaired ¯ower and seed formation. Antisense inhibition of SHL expression gives rise to dwar®sm and delayed development. In-frame N-terminal fusion of the SHL protein to b-glucuronidase (GUS) directs GUS to the nucleus of stably transformed Arabidopsis plants. Thus, SHL encodes a novel putative regulator of gene expression, which directly or indirectly in¯uences a broad range of developmental processes. Key words PHD ®nger á BAH domain á Transcription factor á Nuclear localization á Arabidopsis
Introduction Plant transcriptional regulators are characterized by a multitude of structural motifs (Meshi and Iwabuchi 1995; Liu et al. 1999). These include various (putative) zinc-containing motifs, among them the PHD ®ngers (Aasland et al. 1995), which are characterized by a unCommunicated by G. JuÈrgens C. MuÈssig á T. Altmann (&) Max Planck Institut fuÈr Molekulare P¯anzenphysiologie, Dept. Willmitzer, 14424 Potsdam, Germany E-mail: [email protected] Tel.: +49-331-5678256 Fax: +49-331-5678250 A. Kauschmann BASF AG, 67056 Ludwigshafen, Germany S. D. Clouse North Carolina State University, Raleigh, NC 27695, USA
ique Cys4-His-Cys3 pattern, spanning approximately 50± 80 amino acids. The arrangement of cysteine, histidine, and other residues distinguishes this motif from the similarly sized RING ®ngers (Saurin et al. 1996) and LIM domains (SaÂnchez-Garcia and Rabbitts 1994). The name ``PHD ®nger'' refers to the Cys-rich regions of the two plant homeodomain proteins HAT3.1 of Arabidopsis and Zmhox1a of maize (Schindler et al. 1993). Other PHD ®nger-containing plant proteins are PRHP and PRHA (pathogenesis-related homeodomain proteins from parsley and Arabidopsis; Korfhage et al. 1994), which may be involved in the transcriptional regulation of pathogen defense-related genes. The function of another plant PHD ®nger protein, ES43 from barley (Speulman and Salamini 1995), however, is unknown. In animals PHD ®ngers are also found in transcriptional regulators, including members of the Polycomb and trithorax group of proteins (reviewed by Kennison 1995). The Polycomb group (Pc-G) gene products are transcriptional regulators which silence homeobox-containing (HOM) genes and thus contribute to ensuring the correct expression patterns at speci®c developmental stages (Pirrotta 1997). Trithorax group (trx-G) genes have be
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