The nonconserved N-terminus of protein phosphatases 1 influences its active site.

Abstract:

:Protein phosphatase 1 consists of a secondary structure arrangement, conserved in the serine/threonine protein phosphatase gene family, flanked by nonconserved N-terminal and C-terminal domains. The deletion mutant of PP1 with the 8 nonconserved N-terminal residues removed was designated PP1-(9-330). PP1-(9-330) had a higher activity and affinity than PP1 when assayed against four different substrates, and it also demonstrated a 6-fold higher sensitivity to the inhibitor okadaic acid. This suggested that the N-terminal domain suppressed the activity of PP1 and interfered with its inhibition by okadaic acid. The ANS fluorescence intensity of PP1-(9-330) was greater than that of PP1, which implies that the hydrophobic groove running from active site in the truncated PP1 was more hydrophobic than in PP1. Our findings provide evidence that the nonconserved N-terminus of PP1 functions as an important regulatory domain that influences the active site and its pertinent properties.

journal_name

BMB Rep

journal_title

BMB reports

authors

Xie X,Huang W,Xue C,Wei Q

doi

10.5483/bmbrep.2008.41.12.881

subject

Has Abstract

pub_date

2008-12-31 00:00:00

pages

881-5

issue

12

eissn

1976-6696

issn

1976-670X

journal_volume

41

pub_type

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