Identification of functional domains in the Sep1 protein (= Kem1, Xrn1), which is required for transition through meiotic prophase in Saccharomyces cerevisiae

Chromosoma ◽  
1995 ◽  
Vol 104 (3) ◽  
pp. 215-222 ◽  
Author(s):  
Vladimir I. Bashkirov ◽  
Jachen A. Solinger ◽  
Wolf-Dietrich Heyer
1989 ◽  
Vol 9 (11) ◽  
pp. 4621-4630
Author(s):  
D J Mahoney ◽  
J R Broach

Mating-type genes resident in the silent cassette HML at the left arm of chromosome III are repressed by the action of four SIR gene products, most likely mediated through two cis-acting sites located on opposite sides of the locus. We showed that deletion of either of these two cis-acting sites from the chromosome did not yield any detectable derepression of HML, while deletion of both sites yielded full expression of the locus. In addition, each of these sites was capable of exerting repression of heterologous genes inserted in their vicinity. Thus, HML expression is regulated by two independent silencers, each fully competent for maintaining repression. This situation was distinct from the organization of the other silent locus, HMR, at which a single silencer served as the predominant repressor of expression. Examination of identifiable domains and binding sites within the HML silencers suggested that silencing activity can be achieved by a variety of combinations of various functional domains.


FEBS Letters ◽  
1998 ◽  
Vol 428 (3) ◽  
pp. 281-285 ◽  
Author(s):  
Masatake Iida ◽  
Kunihiko Terada ◽  
Yoshihiro Sambongi ◽  
Tokumitsu Wakabayashi ◽  
Naoyuki Miura ◽  
...  

1990 ◽  
Vol 10 (5) ◽  
pp. 2224-2236
Author(s):  
N Ogawa ◽  
Y Oshima

The PHO4 gene encodes a positive regulatory factor involved in regulating transcription of various genes in the phosphatase regulon of Saccharomyces cerevisiae. Besides its own coding region, the 1.8-kilobase PHO4 transcript contains a coding region for a mitochondrial protein which does not appear to be translated. Four functional domains were found in the PHO4 protein, which consists of 312 amino acid (aa) residues as deduced from the open reading frame of PHO4. A gel retardation assay with beta-galactosidase::PHO4 fused protein revealed that the 85-aa C terminus is the domain responsible for binding to the promoter DNA of PHO5, a gene under the control of PHO4. This region has similarities with the amphipathic helix-loop-helix motif of c-myc protein. Determination of the nucleotide sequences of four PHO4c mutant alleles and insertion and deletion analyses of PHO4 DNA indicated that a region from aa 163 to 202 is involved in interaction with a negative regulatory factor PHO80. Complementation of a pho4 null allele with the modified PHO4 DNAs suggested that the N-terminal region (1 to 109 aa), which is rich in acidic aa, is the transcriptional activation domain. The deleterious effects of various PHO4 mutations on the constitutive transcription of PHO5 in PHO4c mutant cells suggested that the region from aa 203 to 227 is involved in oligomerization of the PHO4 protein.


2007 ◽  
Vol 104 (43) ◽  
pp. 16934-16939 ◽  
Author(s):  
H. Scherthan ◽  
H. Wang ◽  
C. Adelfalk ◽  
E. J. White ◽  
C. Cowan ◽  
...  

Chromosoma ◽  
1994 ◽  
Vol 103 (2) ◽  
pp. 129-141 ◽  
Author(s):  
J�rg B�hler ◽  
Gerrit Hagens ◽  
Gudrun Holzinger ◽  
Harry Scherthan ◽  
Wolf-Dietrich Heyer

1990 ◽  
Vol 4 (7) ◽  
pp. 1141-1148 ◽  
Author(s):  
A Hoffmann ◽  
M Horikoshi ◽  
C K Wang ◽  
S Schroeder ◽  
P A Weil ◽  
...  

1999 ◽  
Vol 19 (12) ◽  
pp. 7933-7943 ◽  
Author(s):  
Jun-Yi Leu ◽  
G. Shirleen Roeder

ABSTRACT The Saccharomyces cerevisiae HOP2 gene is required to prevent formation of synaptonemal complex between nonhomologous chromosomes during meiosis. The HOP2 gene is expressed specifically in meiotic cells, with the transcript reaching maximum abundance early in meiotic prophase. The HOP2 coding region is interrupted by an intron located near the 5′ end of the gene. This intron contains a nonconsensus 5′ splice site (GUUAAGU) that differs from the consensus 5′ splice signal (GUAPyGU) by the insertion of a nucleotide and by a single nucleotide substitution. Bases flanking the HOP2 5′ splice site have the potential to pair with sequences in U1 small nuclear RNA, and mutations disrupting this pairing reduce splicing efficiency. HOP2pre-mRNA is spliced efficiently in the absence of the Mer1 and Nam8 proteins, which are required for splicing the transcripts of two other meiosis-specific genes.


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