GLORIA — GEOMAR Library Ocean Research Information Access

Treffer pro Seite

Treffer 1 - 2 | 2 Treffer

Sortierung

Digitale Medien

Phosphorylation of HMG-I by Protein Kinase C Attenuates Its Binding Affinity to the Promoter Regions of Protein Kinase C γ and Neurogranin/RC3 Genes (2000)

Xiao, Dian-Mo ; Pak, Jhang Ho ; Wang, Xiaoming ; [weitere]

Oxford UK : Blackwell Science Ltd

Journal of neurochemistry 74 (2000), S. 0

zur Merkliste hinzufügen auf der Merkliste

Details

ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: Abstract: A 20-kDa DNA-binding protein that binds the AT-rich sequences within the promoters of the brain-specific protein kinase C (PKC) γ and neurogranin/RC3 genes has been characterized as chromosomal nonhistone high-mobility-group protein (HMG)-I. This protein is a substrate of PKC α, β, γ, and δ but is poorly phosphorylated by PKC ε and ζ. Two major (Ser44 and Ser64) and four minor phosphorylation sites have been identified. The extents of phosphorylation of Ser44 and Ser64 were 1:1, whereas those of the four minor sites all together were 〈30% of the major one. These PKC phosphorylation sites are distinct from those phosphorylated by cdc2 kinase, which phosphorylates Thr53 and Thr78. Phosphorylation of HMG-I by PKC resulted in a reduction of DNA-binding affinity by 28-fold as compared with 12-fold caused by the phosphorylation with cdc2 kinase. HMG-I could be additively phosphorylated by cdc2 kinase and PKC, and the resulting doubly phosphorylated protein exhibited a 〉 100-fold reduction in binding affinity. The two cdc2 kinase phosphorylation sites of HMG-I are adjacent to the N terminus of two of the three predicted DNA-binding domains. In comparison, one of the major PKC phosphorylation sites, Ser64, is adjacent to the C terminus of the second DNA-binding domain, whereas Ser44 is located within the spanning region between the first and second DNA-binding domains. The current results suggest that phosphorylation of the mammalian HMG-I by PKC alone or in combination with cdc2 kinase provides an effective mechanism for the regulation of HMG-I function.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1046/j.1471-4159.2000.0740392.x

Permalink

	Standort	Signatur	Einschränkungen	Verfügbarkeit

Andere fanden auch interessant ...

Artikel (Nationallizenzen)

Volltext

Digitale Medien

Predicted sequence and structure of a vegetative lectin in Pisum sativum (1992)

Pak, Jhang Ho ; Hendrickson, Thomas ; Dobres, Michael S.

Springer

Plant molecular biology 18 (1992), S. 857-863

zur Merkliste hinzufügen auf der Merkliste

Details

ISSN: 1573-5028

Schlagwort(e): lectin ; legume ; pea

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: Abstract We report the predicted sequence of four vegetative homologues (Blec1,2,3 and 4) of the pea seed lectin. This study indicates that, in contrast to the single-copy pea seed lectin (Kaminski et al., Plant Mol Biol 9: 497–507, 1987), the pea vegetative lectin is transcribed by at least four members of a highly conserved multigene family whose members are only distantly related to the pea seed lectin at the primary amino-acid sequence level. For example, Blec1 shares only 38% amino-acid identity with the pea seed lectin. However, molecular homology modelling predicts that Blec1 probably forms a similar tertiary structure to the pea seed lectin.