PMID- 10514485
OWN - NLM
STAT- MEDLINE
DCOM- 19991119
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 42
DP  - 1999 Oct 15
TI  - Prenylated prelamin A interacts with Narf, a novel nuclear protein.
PG  - 30008-18
AB  - Prelamin A is farnesylated and methylated on the cysteine residue of a
      carboxyl-terminal CaaX motif. In the nucleus, prelamin A is processed to lamin A 
      by endoproteolytic removal of the final 18 amino acids, including the
      farnesylated cysteine residue. Using the yeast two-hybrid assay, we isolated a
      novel human protein, Narf, that binds the carboxyl-terminal tail of prelamin A.
      Narf has limited homology to iron-only bacterial hydrogenases and eukaryotic
      proteins of unknown function. Narf is encoded by a 2-kilobase mRNA expressed in
      all human cell lines and tissues examined. The protein is detected in the nuclear
      fraction of HeLa cell lysates on Western blots and can be extracted from nuclear 
      envelopes with 0.5 M NaCl. When a FLAG epitope-tagged Narf is expressed in HeLa
      cells, it is exclusively nuclear and partially co-localizes with the nuclear
      lamina. The farnesylation status of prelamin A determines its ability to bind to 
      Narf. Inhibition of farnesyltransferase and mutation or deletion of the CaaX
      motif from the prelamin A tail domain inhibits Narf binding in yeast two-hybrid
      and in vitro binding assays. The prenyl-dependent binding of Narf to prelamin A
      is an important first step in understanding the functional significance of the
      lamin A precursor.
FAU - Barton, R M
AU  - Barton RM
AD  - Department of Medicine, College of Physicians and Surgeons, Columbia University, 
      New York, New York 10032, USA. hjw14@columbia.edu
FAU - Worman, H J
AU  - Worman HJ
LA  - eng
SI  - GENBANK/AF128406
GR  - 1S10-RR10506/RR/NCRR NIH HHS/United States
GR  - 5-P30-CA13696/CA/NCI NIH HHS/United States
GR  - CA66974/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Laminin)
RN  - 0 (Narf protein, human)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Protein Precursors)
RN  - 151186-83-3 (laminin A)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Cell Nucleus/metabolism
MH  - DNA, Complementary
MH  - HeLa Cells
MH  - Humans
MH  - Laminin/*metabolism
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/chemistry/genetics/*metabolism
MH  - Protein Binding
MH  - Protein Precursors/*metabolism
MH  - Protein Prenylation
MH  - Sequence Homology, Amino Acid
EDAT- 1999/10/09 00:00
MHDA- 1999/10/09 00:01
CRDT- 1999/10/09 00:00
PHST- 1999/10/09 00:00 [pubmed]
PHST- 1999/10/09 00:01 [medline]
PHST- 1999/10/09 00:00 [entrez]
AID - 10.1074/jbc.274.42.30008 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 15;274(42):30008-18. doi: 10.1074/jbc.274.42.30008.