Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.27.1 (
RNase
)
16,360
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The recently identified novel protein
SURF-6
is shown to be a component of the nucleolar matrix. Immunofluorescence analysis demonstrated that
SURF-6
was localized in residual nucleoli of in situ nuclear matrix preparations of mouse fibroblast cells (NIH 3T3), which were depleted of soluble and chromatin related proteins. Immunoblot analysis of biochemical nucleolar subfractions confirmed that
SURF-6
was present in the nucleolar matrix fraction, and was absent from the fractions of soluble proteins released by DNase or
RNase
. The capacity of
SURF-6
to bind nucleic acids was investigated in vitro. Both endogenous
SURF-6
from nuclear extracts and recombinant
SURF-6
exhibited a strong binding capacity for nucleic acids. It was shown that
SURF-6
bound to both DNA and RNA, however, it showed stronger binding to RNA. The presence and nuclear distribution of
SURF-6
during the cell cycle was explored by immunofluorescence analysis. It was shown that
SURF-6
was always found in the nucleolus regardless of the phase of the cell cycle suggesting that it is a structural protein constitutively present in nucleolar substructures. The colocalization of
SURF-6
with the major nucleolar proteins B23 and fibrillarin, which are known to be involved in the processing of ribosomal RNA (rRNA), was examined both in interphase and mitosis by double immunolabeling of cells.
SURF-6
was found to be largely coincident with both proteins in interphase and it was distributed in the same cellular locations, namely the perichromosomal layer, the cytoplasm and prenucleolar bodies, in mitosis. However, colocalization of
SURF-6
with fibrillarin and B23 was only partial in interphase, and the dynamics of its localization was not completely the same as those of either fibrillarin or B23 during mitosis. Taken together, these results indicate that
SURF-6
is a novel nucleolar matrix component and imply that
SURF-6
might support nucleolar matrix structure and function(s) via its association with nucleic acids. We propose that
SURF-6
may be involved in processing of rRNA, based on its cytological characteristics, but at stages in ribosomal biogenesis which are different from those for fibrillarin and B23.
...
PMID:The SURF-6 protein is a component of the nucleolar matrix and has a high binding capacity for nucleic acids in vitro. 954 74