Polyphosphate as a source of phosphoryl group in protein modification in the archaebacterium Sulfolobus acidocaldarius.

Abstract:

:The incubation of polyphosphates with the ribosomal fraction of Sulfolobus acidocaldarius leads to the covalent attachment of phosphate to threonine residue(s) of a single 40,000 Mr protein. The hydrolysis kinetics of this protein showed that polyphosphate might be the modifying group. The reaction requires 2 mM Mn2+ ions and is time-dependent. ATP strongly inhibits the transfer of phosphate from polyphosphate, indicating that this process is catalyzed by an enzyme differing from the well-known protein kinases.

journal_name

Biochimie

journal_title

Biochimie

authors

Skorko R

doi

10.1016/0300-9084(89)90115-6

subject

Has Abstract

pub_date

1989-09-01 00:00:00

pages

1089-93

issue

9-10

eissn

0300-9084

issn

1638-6183

pii

0300-9084(89)90115-6

journal_volume

71

pub_type

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