Analysis of the polyadenylation consensus sequence context in the genes of nuclear encoded mitochondrial proteins

Juretić, Nenad; Theus, Michael

doi:10.1016/0014-5793(91)81212-q

Cited by 17 publications

(7 citation statements)

References 107 publications

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“…The amino acid composition of the first 53 amino acids in the predicted hsp78 sequence is consistent with the properties of known mitochondrial leader peptides (46). Two TATA boxlike sequences are present at positions -103 and -93 in the 5' upstream sequence (61), and the polyadenylation signals TACATA (47) and AATAAA (25) are present in the downstream sequence. In addition, the sequence between positions -247 and -230 matches a characteristic heat shock regulatory element containing GAA segments repeated at 2-nucleotide intervals in alternating orientations (1,66).…”

Section: Resultssupporting

confidence: 68%

HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases.

Leonhardt¹,

Fearson²,

Danese³

et al. 1993

Mol. Cell. Biol.

104

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The Saccharomyces cerevisiae nuclear gene for a 78-kDa mitochondrial heat shock protein (hsp78) was identified in a Agtll expression library through immunological screening with an hsp78-specific monoclonal antibody. Cells exposed to physiological stress, such as an abrupt elevation in temperature, synthesize a subset of highly conserved cellular proteins collectively known as the heat shock or stress proteins. Many members of the heat shock protein (HSP) families are expressed in the absence of stress and function as molecular chaperones in the folding of newly synthesized polypeptide chains and in the assembly of oligomeric structures (for recent reviews, see references 2 and 13). Heat shock proteins also appear to be involved in the degradation of unfolded or damaged polypeptides, either by catalyzing proteolysis or by presenting polypeptides to the active proteases. Well-known examples of heat-shockinducible proteins involved in protein degradation are ubiquitin in eukaryotes (55) and the ATP-dependent La (Lon) and ClpP proteases in prokaryotes (4,30). In addition, members of the newly discovered family of Clp proteins appear to combine an involvement in proteolysis with many of the characteristics of molecular chaperones, i.e., several are heat shock proteins, they are highly conserved in both prokaryotes and eukaryotes, and in eukaryotes, multiple forms or subfamilies appear to be partitioned in different cellular compartments.The wide distribution of the Clp family of proteins became apparent when the sequence of the ClpA subunit of the two-component ClpA-ClpP ATP-dependent protease (18), also known as the Ti protease (21), was found to be related to a number of previously described proteins with known sequences but unknown functions. These proteins, now * Corresponding author. t Present address:

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Section: Resultssupporting

confidence: 68%

HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases.

Leonhardt¹,

Fearson²,

Danese³

et al. 1993

Mol. Cell. Biol.

104

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“…The 1,831-bp cDNA for clone CYP28A1 and the 1,764-bp cDNA for clone CYP28A2 contain open reading frames encoding proteins of 506 and 505 residues, respectively. The 3Ј untranslated regions of CYP28A1 and CYP28A2 both contain a putative polyadenylation signal [AATAAT and AATAAA, respectively (27)] within 15 bases of the poly(A) tail.…”

Section: Resultsmentioning

confidence: 99%

Molecular cloning of a family of xenobiotic-inducible drosophilid cytochrome P450s: Evidence for involvement in host-plant allelochemical resistance

Danielson

MacIntyre

Fogleman

1997

Proc. Natl. Acad. Sci. U.S.A.

114

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Cytochrome P450s constitute a superfamily of genes encoding mostly microsomal hemoproteins that play a dominant role in the metabolism of a wide variety of both endogenous and foreign compounds. In insects, xenobiotic metabolism (i.e., metabolism of insecticides and toxic natural plant compounds) is known to involve members of the CYP6 family of cytochrome P450s. Use of a 3 RACE (rapid amplification of cDNA ends) strategy with a degenerate primer based on the conserved cytochrome P450 heme-binding decapeptide loop resulted in the amplification of four cDNA sequences representing another family of cytochrome P450 genes (CYP28) from two species of isoquinoline alkaloidresistant Drosophila and the cosmopolitan species Drosophila hydei. The CYP28 family forms a monophyletic clade with strong regional homologies to the vertebrate CYP3 family and the insect CYP6 family (both of which are involved in xenobiotic metabolism) and to the insect CYP9 family (of unknown function). Induction of mRNA levels for three of the CYP28 cytochrome P450s by toxic host-plant allelochemicals (up to 11.5-fold) and phenobarbital (up to 49-fold) corroborates previous in vitro metabolism studies and suggests a potentially important role for the CYP28 family in determining patterns of insect-host-plant relationships through xenobiotic detoxification.

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“…The secondary structure for the 3ЈUTR of ATM1 and other nuclearly encoded mitochondrial genes predicted several long and stable doublestranded regions. Additionally, for all of them the AU content is approximately 70%, a finding which is reminiscent of the highly conserved 3ЈUTR of nucleus-encoded mitochondrial proteins of rat liver (28). It has been shown that the 3ЈUTR of the ␤1-F1 ATPase transcript is involved in controlling the translation, stability, and subcellular localization of the mRNA during rat liver development (18).…”

Section: Discussionmentioning

confidence: 96%

“…To better characterize the nucleotide sequence within the 3ЈUTR of ATM1 responsible for mRNA transport to mitochondrion-bound polysomes, the regions between the stop codon and the canonical polyadenylation signal sequence AATAAA (28) were shortened by 97 and 238 bp, respectively (Fig. 6B).…”

Section: Fig 3 Expression and Localization Of Gfp-atm1p Chimeras (A)mentioning

confidence: 99%

In Yeast, the 3′ Untranslated Region or the Presequence of ATM1 Is Required for the Exclusive Localization of Its mRNA to the Vicinity of Mitochondria

Corral‐Debrinski

Blugeon

Jacq

2000

Molecular and Cellular Biology

130

137

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We isolated mitochondria from Saccharomyces cerevisiae to selectively study polysomes bound to the mitochondrial surface. The distribution of several mRNAs coding for mitochondrial proteins was examined in free and mitochondrion-bound polysomes. Some mRNAs exclusively localize to mitochondrion-bound polysomes, such as the ones coding for Atm1p, Cox10p, Tim44p, Atp2p, and Cot1p. In contrast, mRNAs encoding Cox6p, Cox5a, Aac1p, and Mir1p are found enriched in free cytoplasmic polysome fractions. Aac1p and Mir1p are transporters that lack cleavable presequences. Sequences required for mRNA asymmetric subcellular distribution were determined by analyzing the localization of reporter mRNAs containing the presequence coding region and/or the 3-untranslated region (3UTR) of ATM1, a gene encoding an ABC transporter of the mitochondrial inner membrane. Biochemical analyses of mitochondrion-bound polysomes and direct visualization of RNA localization in living yeast cells allowed us to demonstrate that either the presequence coding region or the 3UTR of ATM1 is sufficient to allow the reporter mRNA to localize to the vicinity of the mitochondrion, independently of its translation. These data demonstrate that mRNA localization is one of the mechanisms used, in yeast, for segregating mitochondrial proteins.

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Analysis of the polyadenylation consensus sequence context in the genes of nuclear encoded mitochondrial proteins

Cited by 17 publications

References 107 publications

HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases.

HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases.

Molecular cloning of a family of xenobiotic-inducible drosophilid cytochrome P450s: Evidence for involvement in host-plant allelochemical resistance

In Yeast, the 3′ Untranslated Region or the Presequence of ATM1 Is Required for the Exclusive Localization of Its mRNA to the Vicinity of Mitochondria

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