http://mcdb.colorado.edu daily 1 2009-01-15T21:57:51Z http://mcdb.colorado.edu/mcdb/wood/bill-wood-publications/EdgarEtAl2001 Previous work has shown that the Caenorhabditis elegans gene pal-1, a homolog ofDrosophila caudal, is required maternally for blastomere specification in the early embryo and postembryonically for tail development in males. We show here that embryonic (zygotic) transcription of pal-1 is also required for posterior patterning during later embryogenesis. Embryos homozygous for strong loss-of-function mutations arrest as nonviable L1 larvae with gross posterior defects. PAL-1 protein produced from zygotic transcripts is expressed dynamically during gastrulation and morphogenesis in specific cells of all major lineages except the germ line. Most expressing cells are undergoing cell movements or forming midline structures or both. Mutant embryos exhibit defects involving most of the expressing cells. Aberrant early cell positions are observed in posteriorhypodermis, both in the C-lineage cells that express pal-1 and in the neighboring hypodermal seam cell precursors, which do not, as well as in posterior muscle derived from the C and D lineages. Defects in late gastrulation, ventral hypodermal enclosure, and formation of the rectum result from failures of cell movements of ABp and MS descendants. Limited mosaic analysis supports the view that most of the required pal-1 functions are cell autonomous. No publisher admin 2009-01-13T19:51:44Z Article Reference http://mcdb.colorado.edu/journal-clubs/cell-biology-journal-club/papers/Zito%20et%20al%20SUPP.pdf No publisher vonderfe 2009-10-30T20:28:35Z File http://mcdb.colorado.edu/journal-clubs/cell-biology-journal-club/papers/Zito%20et%20al.pdf No publisher vonderfe 2009-10-30T20:27:58Z File http://mcdb.colorado.edu/mcdb/lgold/Larry%20Gold%20Publications/GaussEtAl1987 The DNA binding domain of the gene 32 protein of the bacteriophage T4 contains asingle "zinc-finger" sequence. The gene 32 protein is an extensively studied member of a class of proteins that bind relatively nonspecifically to single-stranded DNA. We have sequenced and characterized mutations in gene 32 whose defective proteins are activated by increasing the Zn(II) concentration inthe growth medium. Our results identify a role for the gene 32 protein in activation of T4 late transcription. Several eukaryotic proteins with zinc fingers participate in activation of transcription, and the gene 32 protein of T4 should provide a simple, well-characterized system in which genetics can be utilized to study the role of a zinc finger in nucleic acid binding and gene expression. No publisher admin 2009-01-13T21:14:00Z Article Reference http://mcdb.colorado.edu/mcdb/boswell/Robert%20Boswell%20Publications/MohrBoswell1999 The related mouse proteins Miz1 and PIAS3, which have predicted zinc finger domains, interact with the transcription factors Msx2 and STAT3, modulating the ability of Msx2 and STAT3 to regulate transcription. Here, we describe a Drosophila gene, zimp, that encodes a protein with similarity to Miz1 and PIAS3.The zimp gene appears to be post-transcriptionally regulated, as three alternatively spliced forms are detected in a cDNA library screen and on an RNA blot. In addition, all three zimp transcripts are detected in embryonic mRNA, but only two of the transcripts are detected in adult mRNA. The three transcripts have the ability to encode two proteins, of 554 and 522 amino acids. The two Zimp amino acid sequences share an amino-terminal 515-amino-acid region and differ intheir carboxy-termini. These proteins and related proteins in other organisms, including mammals, C. elegans, yeast, and plants, share a highly conserved region predicted to form a zinc finger. Deletion of the zimp gene or P-element insertion in zimp is lethal; thus, zimp is an essential gene in Drosophila. These data underscore the potential importance of Zimp-related proteins cross-species, and conservation of the putative zinc finger domain suggests that it is functionallyimportant. No publisher admin 2009-01-13T17:49:46Z Article Reference http://mcdb.colorado.edu/mcdb/zzzhang No publisher myuan 2008-08-04T17:08:55Z Person http://mcdb.colorado.edu/mcdb/andrysik No publisher admin 2009-06-19T17:19:49Z Person http://mcdb.colorado.edu/mcdb/yhan No publisher admin 2009-06-19T20:07:24Z Person http://mcdb.colorado.edu/facilities/mcdbit/software-request-1/replyto No publisher admin 2009-06-08T20:44:47Z String Field http://mcdb.colorado.edu/facilities/mcdbit/ftp-server-account-request/replyto No publisher admin 2009-05-21T03:53:04Z String Field http://mcdb.colorado.edu/undergraduate/undergraduate-lab-experience/replyto No publisher admin 2009-01-17T03:12:02Z String Field http://mcdb.colorado.edu/facilities/flow-cytometry-facility/fcf-appointment-cancellation-form/replyto No publisher admin 2009-02-10T19:10:41Z String Field http://mcdb.colorado.edu/facilities/flow-cytometry-facility/fcf-booking-form/investigator-information/replyto No publisher admin 2009-02-10T17:51:57Z String Field http://mcdb.colorado.edu/mcdb/yyshi No publisher myuan 2008-08-07T17:00:20Z Person http://mcdb.colorado.edu/mcdb/leinwand/Leslie%20Leinwand%20Publications/MarinerEtAl2005 In the work presented here, we elucidate a mechanism for the repression of alpha-myosin heavy chain (MyHC) during pathological cardiac hypertrophy. We demonstrate that the transcription factor Yin Yang 1 (YY1) significantly decreases endogenous alpha-MyHC mRNA and protein expression in neonatal rat ventricular myocytes. Furthermore, mutation of the YY1 binding sites in the proximal rat alpha-MyHC promoter increases promoter activity and alleviates YY1-mediated repression of the promoter. Despite the presence of 5 sites that bind YY1, only one site, located at -94bp of the rat alpha-MyHC promoter, is both necessary and sufficient for pathological repression of the promoter by phorbol esters, revealing a unique mechanism for the repression of alpha-MyHC expressionduring cardiac hypertrophy. No publisher zyuan 2009-01-14T19:18:16Z Article Reference