Non-dependence on native structure of pig liver pyruvate kinase when used as a substrate for cyclic 3′,5′-AMP-stimulated protein kinase

Humble, Elisabet; Berglund, Lars; Titanji, Vincent P. K.; Ljungström, Olle; Edlund, Bror; Zetterqvist, Örjan; Engström, Lorentz

doi:10.1016/0006-291x(75)90554-9

Cited by 62 publications

(21 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…These ideas were supported by the work of Daile & Carnegie (1974), who showed that several basic peptides produced by thermolytic or peptic digestion of myelin basic protein were almost as good substrates as was the undigested protein. A similar result was obtained by Humble et al (1975), who found that a peptide produced by digestion of L-type pyruvate kinase with CNBr was a better substrate than the native enzyme. However, in our earlier work we reported that the amino acid sequences of two tryptic peptides around the two phosphorylation sites on phosphorylase kinase phosphorylated in vivo resembled neither each other nor the sequence round the histone Hi site (Langan, 1969(Langan, , 1971Cohen et al, 1975;Yeaman & Cohen, 1975).…”

supporting

confidence: 83%

“…They found that lysozyme, serum albumin, creatine kinase and phosphorylase b were not substrates when they were in their native states, but that they became substrates when they had been subjected to reduction, carboxymethylation and maleylation. Similarly, Humble et al (1975) showed that L-type pyruvate kinase became a better substrate for cyclic AMP-dependent protein kinase after it had been denatured in alkali. These results suggested that some feature of the substrate's primary structure rather than its tertiary structure must be important in determining whether it can be phosphorylated, and that the native con-formation of the,substrate may only be important in a negative sense in that it may prevent the phosphorylation of an otherwise suitable residue.…”

mentioning

confidence: 98%

See 1 more Smart Citation

The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

Yeaman¹,

Cohen²,

Watson³

et al. 1977

Biochemical Journal

144

View full text Add to dashboard Cite

The known amino acid sequences at the two sites on phosphorylase kinase that are phosphorylated by cyclic AMP-dependent protein kinase were extended. The sequences of 42 amino acids around the phosphorylation site on the a-subunit and of 14 amino acids around the phosphorylation site on the fl.subunit were shown to be: a-subunit Phe-Arg-Arg-Leu-Ser(P)-I1e-Ser-Thr-Glu-Ser-Glx-Pro-Asx-Gly-Gly-His-Ser-Leu-GlyAla-Asp-Leu-Met-Ser-Pro-Ser-Phe-Leu-Ser-Pro-Gly-Th.r-Ser-Val-Phe(Ser,Pro,Gly)HisThr-Ser-Lys; 1)-subunit, Ala-Arg-Thr-Lys-Arg-Ser-Gly-Vr()alTyr-Glu-Pro-LeuLys. The sites on histone H2B which are phosphorylated by cyclic AMP-dependent protein kinase in vitro were identified as serine-36 and serine-32. The amino acid sequence 32 36 in this region is:

show abstract

supporting

confidence: 83%

mentioning

confidence: 98%

The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

Yeaman¹,

Cohen²,

Watson³

et al. 1977

Biochemical Journal

144

View full text Add to dashboard Cite

show abstract

“…The primary sequence may not be the specificity determinant for the recognition of eIF-2a by HCR since Kramer and Hardesty [48] have reported that denatured eIF-2 is a poor substrate for HCR, suggesting that features of the secondary or tertiary structure of eIF-2 may be important for this. This is in contrast to phosphorylation of proteins by CAMP-dependent protein kinase where denaturation has been shown to make proteins better substrates for this enzyme [49]. However, the large number of PSI).…”

Section: Discussionmentioning

confidence: 94%

Structure and regulation of eukaryotic initiation factor eIF-2. Sequence of the site in the alpha subunit phosphorylated by the haem-controlled repressor and by the double-stranded RNA-activated inhibitor

1987

View full text Add to dashboard Cite

Eukaryotic protein synthesis initiation factor 2 (eIF-2) can be phosphorylated on its tl subunit by two wellcharacterised protein kinases, termed the haem-controlled repressor (HCR) and the double-stranded RNAactivated inhibitor (dsI). Phosphorylation of eIF-2 by these kinases is thought to be important in the regulation of peptide-chain initiation. We report the location of the serine residue in the a subunit, which is phosphorylated by both these enzymes. Limited tryptic digestion and subsequent cyanogen bromide treatment of rat liver eIF-2 phosphorylated by HCR yielded one major phosphopeptide. This peptide had the sequence Ile-Leu-Leu-Ser-Glu-Leu-Ser(P)-Arg-Arg .The same major phosphopeptide was obtained from rabbit reticulocyte eIF-2 phosphorylated by HCR or dsl as judged by its behaviour on two-dimensional mapping and reverse-phase chromatography. In all cases the phosphorylated residue was found to be serine-7, and not serine-4, of the above sequence as determined from sequence analysis and by subdigestion of the peptide with Staphylococcus aureus V8 proteinase.Protein synthesis initiation factor-2 (eIF-2) mediates the binding of the initiator tRNA (Met-tRNAi) to the 40s ribosomal subunit during peptide-chain initiation. The activity of eIF-2 is believed to be important in controlling the overall rate of chain initiation and is regulated by phosphorylation of its smallest (a) subunit (reviewed in [l-31). Briefly, phosphorylation of eIF-2a impairs the recycling of eIF-2 which is required to regenerate active eIF-2 from the inactive [eIF-2 . GDP] complexes which are released from the ribosome after each round of chain initiation [4]. This recycling is mediated by an additional initiation factor [5 -91 termed GEF (guanine-nucleotide-exchange factor). This factor promotes the exchange of bound GDP for GTP and yields the active [eIF-2 . GTP] species, which can bind the initiator Met-tRNA, and participate in a further round of chain initiation.The role of the phosphorylation of eIF-2a in the control of translation has been studied extensively in reticulocytes, where haem deprivation rapidly leads to inhibition of chain initiation associated with increased phosphorylation of eIF-2a. This results from the activation of a haem-regulated

show abstract

“…Recently it has been shown that the PK of rat, chicken and pig liver can be phosphorylated with ATP by a CAMP stimulated protein kinase [7-91 , a process showing similarities to the inhibition of the PK of the snail with PArg and the cationic protein. The time constant of inhibition is rather similar for the snail and for the pig enzyme [9] , and at pH 6.0 PArg increases the sigmoidicity of the kinetics of the snail enzyme in the same way as ATP in the presence of a protein kinase increases the sigmoidicity of rat liver PK at pH 7.0 [8].…”

mentioning

confidence: 75%

Inhibition of the pyruvate kinase of Helix pomatia L. By phospho‐L‐arginine Phosphorylation or a novel mechanism?

Wieser¹,

Lackner²

1977

FEBS Letters

View full text Add to dashboard Cite

Non-dependence on native structure of pig liver pyruvate kinase when used as a substrate for cyclic 3′,5′-AMP-stimulated protein kinase

Cited by 62 publications

References 22 publications

The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

Structure and regulation of eukaryotic initiation factor eIF-2. Sequence of the site in the alpha subunit phosphorylated by the haem-controlled repressor and by the double-stranded RNA-activated inhibitor

Inhibition of the pyruvate kinase of Helix pomatia L. By phospho‐L‐arginine Phosphorylation or a novel mechanism?

Contact Info

Product

Resources

About